EP4695310A1 - Hybrid polymer comprising a polysaccharide polymer and peptide chains - Google Patents

Abstract

The present invention relates to a hybrid polymer comprising a polysaccharide polymer and peptide chains, to blends, hydrogels and formulations comprising the hybrid polymer, and to the use of the hybrid polymer as a rheology modifying agent.

Description

HYBRID POLYMER COMPRISING A POLYSACCHARIDE POLYMER AND PEPTIDE CHAINS The present invention relates to a hybrid polymer comprising a polysaccharide polymer and peptide chains, to blends, hydrogels and formulations comprising the hybrid polymer, and to the use of the hybrid polymer as a rheology modifying agent. Cleansing and caring for skin and hair is very important for general hygiene, e.g. for removal of unwanted materials such as sebum, oils, dirt, makeup, or for moisturization, coloring or protection. Many cosmetic products require a certain minimum viscosity in order to achieve ease of application to the substrate and/or retention on the substrate to be treated. Many cosmetic products comprise viscosity- increasing or rheology modifying agents. These are often referred to as thickening agents, thickeners or gelling agents. Thickening agents used in cosmetics or personal care products include polyethylene glycol, polyacrylic acid, vegetable gums, polycarboxylates (Carbopols), homopolymers and copolymers based on 2- acrylamido-2-methyl-1-propanesulfonic acid (AMPS). Many ingredients used in cosmetics are traditionally derived from crude oil. Environmental and economic factors restrict the use of products derived from this limited resource. There is a desire to identify more sustainable and biodegradable, yet gentle and effective materials. Indeed, consumers are interested in natural products including products with a high percentage of natural ingredients and/or ingredients that are derived from renewable materials. Consumers perceive products derived from natural materials to be gentler and more environmentally friendly. Ingredients derived from renewable materials have various other benefits such as increased biodegradability and more sustainable availability. Compounds derived from plant-based resources are particularly useful because the source compound can simply be regrown. WO2018/108663, WO2018/108664, WO2018/108665, and WO2018/108667 disclose water-soluble and/or water-swellable hybrid polymers comprising a polysaccharide polymer and a synthetic polymer. There is an ongoing need for polymeric rheology modifiers that can provide the excellent performance of modern polymers with the increased biodegradability and the more sustainable availability of natural-based polymers. It has now been found that hybrid polymers comprising a polysaccharide polymer and peptide chains are useful as rheology modifying agents. The present invention relates to a hybrid polymer comprising (a) a polysaccharide polymer; and (b) peptide chains. The hybrid polymers of the invention show excellent performance as rheology modifying agents. They form hydrogels having the desired properties. Advantageously, the hybrid polymers of the invention have a high renewable carbon content and are readily biodegradable, i.e., they are sustainable. The hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b) peptide chains. Preferably, the combined amount of (a) the polysaccharide polymer and (b) the peptide chains in the hybrid polymer is at least 50 wt-%, more preferably at least 60 wt-%, more preferably at least 70 wt-%, more preferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably at least 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least 95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt-%, particularly preferably at least 99 wt-%, based on the total weight of the hybrid polymer. The hybrid polymer of the invention comprises a polysaccharide polymer. Preferably, the polysaccharide polymer is water-soluble and/or water-swellable. In at least one embodiment, the polysaccharide polymer absorbs water and/or forms a gel or gum when immersed in water. In at least one embodiment, the polysaccharide polymer is a natural gum. Natural gums are useful because they are generally soluble in water due to the presence of an excessive number of OH groups which form hydrogen bonds with water molecules. In at least one embodiment, the polysaccharide polymer is a natural gum derived from a plant. In preferred embodiments, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, chitosan, xanthan gum, fenugreek gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose, amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karaya gum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotium gum, gellan gum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin, derivatives thereof and mixtures thereof. In more preferred embodiments, the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin, sclerotium gum, gellan gum, diutan gum, inulin, derivatives thereof and mixtures thereof. In even more preferred embodiments, the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, starch, amylose, amylopectin, konjac gum, inulin, derivatives thereof and mixtures thereof. In particularly preferred embodiments, the polysaccharide polymer is dextran. Derivatives of the above polysaccharide polymers may also be used. “Derivative” means that the polysaccharide polymer was subjected to one or more suitable physical, chemical or enzymatic processes to be converted into a derivative of the polysaccharide polymer. Examples of such processes include: - acidic treatment of polysaccharide polymer by the reaction with acids (e.g. hydrochloric acid, phosphoric acid, or sulfuric acid) - alkaline treatment of polysaccharide polymer by the reaction with bases (e.g. sodium hydroxide or potassium hydroxide) - bleached polysaccharide polymer by the reaction with peracetic acid, hydrogen peroxide, sodium hypochlorite, sulfur dioxide, sulfites, potassium permanganate or ammonium persulfate - enzymatic modification of the polysaccharide polymer by treatment with enzymes - oxidized polysaccharide polymer by oxidation (e.g. with sodium hypochlorite) - acetylated polysaccharide polymer by esterification with e.g. anhydrides - hydroxypropyl polysaccharide polymer by reaction with propylene oxide - hydroxyethyl polysaccharide polymer by reaction with ethylene oxide - carboxymethylation of the polysaccharide polymer - glycol polysaccharide polymer Preferred derivatives of the polysaccharide polymers are selected from carboxymethyl polysaccharides, hydroxyethyl polysaccharides, carboxymethyl hydroxyethyl polysaccharides, carboxypropyl polysaccharides, glycol polysaccharides, and mixtures thereof. Examples of preferred derivatives of the polysaccharide polymers are carboxymethyl cellulose, hydroxyethyl cellulose, carboxymethyl hydroxyethyl cellulose, carboxypropyl cellulose, carboxymethyl chitosan, glycol chitosan, or mixtures thereof. In preferred embodiments, the polysaccharide polymer has a weight average molecular weight of from 3000 to 12000000 g/mol, preferably from 10000 to 5000000 g/mol, more preferably from 30000 to 2000000 g/mol, even more preferably from 50000 to 1000000 g/mol, particularly preferably from 100000 to 500000 g/mol. In preferred embodiments, the polysaccharide polymer has a weight average molecular weight of from 3000 to 1000000 g/mol, preferably from 10000 to 500000 g/mol, more preferably from 20000 to 300000 g/mol, even more preferably from 30000 to 200000 g/mol, particularly preferably from 40000 to 150000 g/mol. In a preferred embodiment, the polysaccharide polymer has a weight average molecular weight of from 15000 to 75000 g/mol, preferably from 20000 to 70000 g/mol, more preferably from 20000 to 60000 g/mol, more preferably from 30000 to 60000 g/mol, even more preferably from 30000 to 50000 g/mol, even more preferably from 35000 to 45000 g/mol, for example 40000 g/mol. In a preferred embodiment, the polysaccharide polymer has a weight average molecular weight of from 100000 to 200000 g/mol, preferably from 120000 to 180000 g/mol, more preferably from 130000 to 170000 g/mol, even more preferably from 140000 to 160000 g/mol, for example 150000 g/mol. In a preferred embodiment, the polysaccharide polymer has a weight average molecular weight of at least 180000 g/mol, preferably at least 200000 g/mol. As used herein, the molecular weight, including the weight average molecular weight, of the polysaccharide polymer is determined using gel permeation chromatography (GPC). GPC experiments are performed using a PSS SECcurity² instrument consisting of a pump, autosampler and column oven. A column SUPREMA LIN XL of 300 x 8 mm and 10 µm average particle size is used at a flow rate of 1.0 mL/min and a column temperature of 25°C. As eluent 0.1M NaNO₃ is used. The hybrid polymer of the invention comprises peptide chains. The peptide preferably is a dipeptide, tripeptide, oligopeptide, polypeptide or protein. A person skilled in the art knows what peptides and proteins are. A dipeptide contains two amino acids. A tripeptide contains three amino acids. The oligopeptide preferably contains from four to nine amino acids. The polypeptide preferably contains at least 10 amino acids, more preferably from 10 to 99 amino acids. The protein preferably contains at least 100 amino acids, more preferably from 100 to 30000 amino acids, even more preferably from 100 to 1000 amino acids, particularly preferably from 100 to 300 amino acids. The peptide may also be a hydrolyzed protein. A person skilled in the art knows what a hydrolyzed protein, also referred to as protein hydrolysate, is. A hydrolyzed protein may be obtained by hydrolysis of a protein into peptides and amino acids. Such hydrolysis may be a chemical hydrolysis or an enzymatic hydrolysis. Enzymatic hydrolysis is preferred because it allows for a controlled hydrolysis by targeting specific peptide bonds. The amino acids in the peptide chains may have any stereochemical orientation. For example, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids in the peptide chains are L- amino acids. In one embodiment, all amino acids in the peptide chains are D-amino acids. The amino acids in the peptide chains may optionally be in its salt form. A person skilled in the art knows that this may depend, for example, on the environment of the peptide chains. For example, an acidic environment may lead to protonation of basic functional groups of the side chains of the amino acids. For example, a basic environment may lead to deprotonation of acidic functional groups of the side chains of the amino acids. In preferred embodiments, the peptide chains form aggregates with each other. In preferred embodiments, the peptide chains are self-assembling. Without wishing to be bound by theory: The peptide chains may form noncovalent bonds with each other. The peptide chains may form a supramolecular assembly. This may lead to noncovalent or supramolecular crosslinking, which may lead to gelation. In one embodiment, the peptide chains may form nanofibers or nanofibrillar structures. In one embodiment, the peptide chains may form beta sheets. In preferred embodiments, at least 50%, preferably at least 60%, more preferably at least 70%, even more preferably at least 80%, even more preferably at least 90%, even more preferably at least 95%, particularly preferably at least 98%, of the amino acids in the peptide chains are proteinogenic amino acids. In preferred embodiments, all amino acids in the peptide chains are proteinogenic amino acids. Preferably, the proteinogenic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, lysine, aspartic acid, glutamic acid, arginine, histidine, methionine, serine, threonine, glycine, alanine, proline, cysteine, asparagine, glutamine, selenocysteine, and pyrrolysine. More preferably, the proteinogenic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, lysine, aspartic acid, glutamic acid, arginine, histidine, methionine, serine, threonine, glycine, alanine, proline, cysteine, asparagine, and glutamine. The peptide chains may optionally contain further amino acids F. In embodiments, at most 50%, preferably at most 40%, more preferably at most 30%, even more preferably at most 20%, even more preferably at most 10%, even more preferably at most 5%, particularly preferably at most 2%, of the amino acids in the peptide chains are further amino acids F. In embodiments, the peptide chains do not contain any further amino acids F. Preferably, the further amino acids F are amino acids other than proteinogenic amino acids. Preferably, the further amino acids F are selected from fluorine-containing amino acids, hydroxy group-containing amino acids other than proteinogenic amino acids, boronic acid-containing amino acids, anthracenyl- containing amino acids, amino acids having C₂-C₁₀ alkyl groups other than proteinogenic amino acids, amino acids having C2-C10 alkenyl groups, and amino acids having C2-C10 alkynyl groups. Preferably, the further amino acids F are selected from azidohomoalanine, acridinylalanine, phenylselenocysteine, sulfoserine, p-iodophenylalanine, bipyridylalanine, dansylalanine, o-nitrobenzyl cysteine, 7- nitroindolinyl-amino acids, propargylglycine, azidonorleucine, 5-bromotryptophan, L- 4’-deoxy-4’-iodophenylalanine, tetrazine alanine, dipyridyl tetrazine serine, hydroxyproline, beta-alanine, citrulline, ornithine, norleucine, 3-nitrotyrosine, nitroarginine, and pyroglutamic acid. In preferred embodiments, at least 25%, preferably at least 30%, of the amino acids in the peptide chains are identical. In preferred embodiments, at least 25%, preferably at least 30%, of the amino acids in the peptide chains are identical and preferably selected from hydrophobic amino acids. In more preferred embodiments, at least 25%, preferably at least 30%, of the amino acids in the peptide chains are identical and selected from hydrophobic amino acids. Preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, and tryptophan. More preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, and valine. Even more preferably, the hydrophobic amino acids are selected from leucine, isoleucine, and phenylalanine. Particularly preferably, the hydrophobic amino acids are isoleucine. In preferred embodiments, at least 15%, preferably at least 20%, of the amino acids in the peptide chains are identical. In preferred embodiments, at least 15%, preferably at least 20%, of the amino acids in the peptide chains are identical and preferably selected from charged amino acids. In more preferred embodiments, at least 15%, preferably at least 20%, of the amino acids in the peptide chains are identical and selected from charged amino acids. Preferably, the charged amino acids are selected from lysine, aspartic acid, glutamic acid, arginine, and histidine. More preferably, the charged amino acids are selected from lysine, aspartic acid, and glutamic acid. Particularly preferably, the charged amino acids are lysine. In preferred embodiments, at least 10%, preferably at least 20%, of the amino acids in the peptide chains are selected from amino acids having an amide group in the side chain. Preferably, the amino acids having an amide group in the side chain are selected from asparagine, glutamine, and mixtures thereof. In preferred embodiments, the peptide chains contain at least one methionine. In preferred embodiments, the peptide chains contain at least one amino acid selected from serine, threonine, and mixtures thereof. In more preferred embodiments, the peptide chains contain at least one serine. In preferred embodiments, at least 40%, preferably at least 45%, of the amino acids in the peptide chains are selected from hydrophobic amino acids. In preferred embodiments, at least 40%, preferably at least 45%, of the amino acids in the peptide chains are selected from hydrophilic amino acids. In more preferred embodiments, at least 40%, preferably at least 45%, of the amino acids in the peptide chains are selected from hydrophobic amino acids, and at least 40%, preferably at least 45%, of the amino acids in the peptide chains are selected from hydrophilic amino acids. Preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, glycine, alanine, proline, and methionine. More preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, and methionine. Even more preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, valine, and methionine. Particularly preferably, the hydrophobic amino acids are selected from isoleucine, phenylalanine, and methionine. Preferably, the hydrophilic amino acids are selected from serine, threonine, cysteine, asparagine, glutamine, lysine, aspartic acid, glutamic acid, arginine, and histidine. More preferably, the hydrophilic amino acids are selected from serine, threonine, cysteine, asparagine, glutamine, lysine, aspartic acid, and glutamic acid. Particularly preferably, the hydrophilic amino acids are selected from serine, cysteine, asparagine, glutamine, lysine, and glutamic acid. In preferred embodiments, at least 80%, preferably at least 90%, of the amino acids in the peptide chains are arranged so that hydrophobic amino acids and hydrophilic amino acids alternate. In a particularly preferred embodiment, the peptide chains are selected from peptide chains of Formula P1, peptide chains of Formula P2, peptide chains of Formula P3, salts thereof, tautomers thereof, salts of tautomers thereof, and mixtures thereof:

Peptide P1 is characterized by the above structure or may be a salt thereof, a tautomer thereof or a salt of a tautomer thereof. Thus, the peptide P1 has the structure CKIKISQINM (SEQ ID NO: 1) in one letter code. The amino acids of peptide P1 may have any stereochemical orientation. For example, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids of peptide P1 are L-amino acids. In one embodiment, all amino acids of peptide P1 are D-amino acids. Peptide P2 is characterized by the above structure or may be a salt thereof, a tautomer thereof or a salt of a tautomer thereof. Thus, the peptide P2 has the structure CEIEISQINM (SEQ ID NO: 2) in one letter code. The amino acids of peptide P2 may have any stereochemical orientation. For example, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids of peptide P2 are L-amino acids. In one embodiment, all amino acids of peptide P2 are D-amino acids. Peptide P3 is characterized by the above structure or may be a salt thereof, a tautomer thereof or a salt of a tautomer thereof. The peptide P3 has the structure CKFKFQF (SEQ ID NO: 3) in one letter code. The amino acids of peptide P3 may have any stereochemical orientation. For example, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids of peptide P3 are L-amino acids. In one embodiment, all amino acids of peptide P3 are D-amino acids. In a preferred embodiment, the peptide chains are depsi peptide chains. A person skilled in the art knows what a depsi peptide is. A depsi peptide is a peptide in which one or more of the amide groups in the peptide chain are replaced by an ester group. Preferably, one to three of the amide groups in the peptide chain are replaced by an ester group. More preferably, one or two of the amide groups in the peptide chain are replaced by an ester group. Particularly preferably, one of the amide groups in the peptide chain is replaced by an ester group. In a preferred embodiment, said ester group is part of a structural unit of Formula D: In a preferred embodiment, the peptide chains contain at least one structural unit of Formula D. Preferably, the structural unit of Formula D is located in the middle of the peptide chain. In a particularly preferred embodiment, the peptide chains are selected from peptide chains of Formula P4, peptide chains of Formula P5, salts thereof, tautomers thereof, salts of tautomers thereof, and mixtures thereof:

The depsi peptide P4 is characterized by the above structure or may be a salt thereof, a tautomer thereof or a salt of a tautomer thereof. Thus, the depsi peptide P4 may also be depicted by the structure: [CKIKI]-O-CH2-C(NH2)-CO-[QINM] The depsi peptide P4 thus contains two peptide moieties of sequence CKIKI (SEQ ID NO: 4) and QINM (SEQ ID NO: 5) each in one letter code. In the aforementioned structure, the peptide moieties are depicted in brackets (“[…]”). The depsi peptide P5 is characterized by the above structure or may be a salt thereof, a tautomer thereof or a salt of a tautomer thereof. Thus, the depsi peptide P5 may also be depicted by the structure: [CEIEI]-O-CH2-C(NH2)-CO-[QINM] The depsi peptide P5 thus contains two peptide moieties of sequence CEIEI (SEQ ID NO: 6) and QINM (SEQ ID NO: 5) each in one letter code. In the aforementioned structure, the peptide moieties are depicted in brackets The amino acids of the peptide moieties comprised in depsi peptides P4 and P5 may have any stereochemical orientation. For example, each amino acid may independently from each other be an L-amino acid or a D-amino acid. In one embodiment, all amino acids of one peptide moiety are L-amino acids. In one embodiment, all amino acid of one peptide moiety are D-amino acids. In one embodiment, all amino acids of both peptide moieties in one depsi peptide are D- amino acids. In one embodiment, all amino acids of both peptide moieties in one depsi peptide are L-amino acids. Structural units of Formula D can rearrange to structural units of Formula S: Peptide chains containing structural units of Formula D can rearrange to peptide chains containing structural units of Formula S. Such a rearrangement may be initiated by adjusting the pH, for example increasing the pH. In one embodiment, the rearrangement may be initiated by adjusting the pH from an acidic pH (e.g. pH 2) to a higher pH, for example a neutral pH (e.g. pH 7). The rearrangement may change the geometry of the peptide chains, for example from kinked to linear. The rearrangement may change the solubility of the peptide chains. The rearrangement may lead to aggregation of the peptide chains. In one embodiment, the peptide chains contain at least one structural unit of Formula L: Preferably, the structural unit of Formula L is located in the middle of the peptide chain. Structural units of Formula L can rearrange to structural units of Formula M: Peptide chains containing structural units of Formula L can rearrange to peptide chains containing structural units of Formula M. Such a rearrangement may be initiated by adjusting the pH, for example increasing the pH. In one embodiment, the rearrangement may be initiated by adjusting the pH from an acidic pH (e.g. pH 2) to a higher pH, for example a neutral pH (e.g. pH 7). The rearrangement may change the geometry of the peptide chains, for example from kinked to linear. The rearrangement may change the solubility of the peptide chains. The rearrangement may lead to aggregation of the peptide chains. In one embodiment, one or more of the amide groups in the peptide chain are replaced by a thioester group. Preferably, one to three of the amide groups in the peptide chain are replaced by a thioester group. More preferably, one or two of the amide groups in the peptide chain are replaced by a thioester group. Particularly preferably, one of the amide groups in the peptide chain is replaced by a thioester group. In a preferred embodiment, said thioester group is part of a structural unit of Formula T: In one embodiment, the peptide chains contain at least one structural unit of Formula T. Preferably, the structural unit of Formula T is located in the middle of the peptide chain. Structural units of Formula T can rearrange to structural units of Formula C: Peptide chains containing structural units of Formula T can rearrange to peptide chains containing structural units of Formula C. Such a rearrangement may be initiated by adjusting the pH, for example increasing the pH. In one embodiment, the rearrangement may be initiated by adjusting the pH from an acidic pH (e.g. pH 2) to a higher pH, for example a neutral pH (e.g. pH 7). The rearrangement may change the geometry of the peptide chains, for example from kinked to linear. The rearrangement may change the solubility of the peptide chains. The rearrangement may lead to aggregation of the peptide chains. The peptide chains may optionally contain an N-protected version of a structural unit of Formula D, L or T. Cleavage of the N-protecting group may induce rearrangement to a structural unit of Formula S, M or C, respectively. The N-protecting group may, for example, be cleaved upon UV radiation. Accordingly, rearrangement may, for example, be induced by UV radiation. The peptide chains may optionally be interrupted by an ether or polyether bridge, by an ethylene glycol or polyethyleneglycol bridge, or by a C3-C6 alkylene bridge. The peptide chains may, for example, be of plant origin, animal origin or human origin, or they may, for example, be viral peptides, proteins or fragments thereof or bacterial peptides, proteins or fragments thereof. In one preferred embodiment, the peptide chains are of plant origin. In preferred embodiments, the peptide chains are selected from pea protein, hydrolyzed pea protein, soy bean protein, hydrolyzed soy bean protein, fava bean protein, hydrolyzed fava bean protein, chickpea protein, e.g. aquafaba, hydrolyzed chickpea protein, wheat protein, hydrolyzed wheat protein, rice protein, hydrolyzed rice protein, whey protein, hydrolyzed whey protein, baobab protein, hydrolyzed baobab protein, collagen protein, hydrolyzed collagen protein, plant collagen-like protein, hydrolyzed plant collagen-like protein, hemp seed protein, hydrolyzed hemp seed protein, jojoba protein, hydrolyzed jojoba protein, keratin protein, hydrolyzed keratin protein, lupine protein, hydrolyzed lupine protein, oat protein, hydrolyzed oat protein, quinoa protein, hydrolyzed quinoa protein, and mixtures thereof. In more preferred embodiments, the peptide chains are selected from pea protein, hydrolyzed pea protein, soy bean protein, hydrolyzed soy bean protein, fava bean protein, hydrolyzed fava bean protein, chickpea protein, e.g. aquafaba, hydrolyzed chickpea protein, wheat protein, hydrolyzed wheat protein, rice protein, hydrolyzed rice protein, whey protein, hydrolyzed whey protein, oat protein, hydrolyzed oat protein, quinoa protein, hydrolyzed quinoa protein, and mixtures thereof. In even more preferred embodiments, the peptide chains are selected from pea protein, hydrolyzed pea protein, oat protein, hydrolyzed oat protein, and mixtures thereof. In one embodiment, the peptide chains are selected from proteins. Preferably, the peptide chains are selected from pea protein, soy bean protein, fava bean protein, chickpea protein, e.g. aquafaba, wheat protein, rice protein, whey protein, baobab protein, collagen protein, plant collagen-like protein, hemp seed protein, jojoba protein, keratin protein, lupine protein, oat protein, quinoa protein, and mixtures thereof. More preferably, the peptide chains are selected from pea protein, soy bean protein, fava bean protein, chickpea protein, e.g. aquafaba, wheat protein, rice protein, whey protein, oat protein, quinoa protein, and mixtures thereof. Even more preferably, the peptide chains are selected from pea protein, oat protein, and mixtures thereof. In another embodiment, the peptide chains are selected from hydrolyzed proteins. Preferably, the peptide chains are selected from hydrolyzed pea protein, hydrolyzed soy bean protein, hydrolyzed fava bean protein, hydrolyzed chickpea protein, hydrolyzed wheat protein, hydrolyzed rice protein, hydrolyzed whey protein, hydrolyzed baobab protein, hydrolyzed collagen protein, hydrolyzed plant collagen- like protein, hydrolyzed hemp seed protein, hydrolyzed jojoba protein, hydrolyzed keratin protein, hydrolyzed lupine protein, hydrolyzed oat protein, hydrolyzed quinoa protein, and mixtures thereof. More preferably, the peptide chains are selected from hydrolyzed pea protein, hydrolyzed soy bean protein, hydrolyzed fava bean protein, hydrolyzed chickpea protein, hydrolyzed wheat protein, hydrolyzed rice protein, hydrolyzed whey protein, hydrolyzed oat protein, hydrolyzed quinoa protein, and mixtures thereof. Even more preferably, the peptide chains are selected from hydrolyzed pea protein, hydrolyzed oat protein, and mixtures thereof. In preferred embodiments, the peptide chains contain from 2 to 5000, preferably from 3 to 4000, more preferably from 4 to 3000, more preferably from 5 to 2000, more preferably from 5 to 1000, even more preferably from 6 to 500, even more preferably from 6 to 100, particularly preferably from 7 to 50, for example from 7 to 10, amino acids. In preferred embodiments, the peptide chains contain from 2 to 100, preferably from 3 to 50, more preferably from 4 to 30, even more preferably from 5 to 20, particularly preferably from 6 to 15, for example from 7 to 10, amino acids. In one embodiment, the peptide chains contain 8 or less amino acids. In one embodiment, the peptide chains contain 10 or more amino acids. In preferred embodiments, the peptide chains contain from 100 to 5000, preferably from 200 to 4000, more preferably from 300 to 3000, even more preferably from 400 to 2000, particularly preferably from 500 to 1000, amino acids. In preferred embodiments, the peptide chains have a weight average molecular weight of from 150 to 600000 g/mol, preferably from 200 to 400000 g/mol, more preferably from 300 to 300000 g/mol, more preferably from 400 to 200000 g/mol, more preferably from 500 to 100000 g/mol, even more preferably from 600 to 50000 g/mol, even more preferably from 700 to 10000 g/mol, particularly preferably from 750 to 5000 g/mol, for example from 800 to 1500 g/mol. In preferred embodiments, the peptide chains have a weight average molecular weight of from 150 to 10000 g/mol, preferably from 300 to 5000 g/mol, more preferably from 500 to 4000 g/mol, even more preferably from 600 to 3000 g/mol, particularly preferably from 700 to 2000 g/mol, for example from 800 to 1500 g/mol. In preferred embodiments, the peptide chains have a weight average molecular weight of from 10000 to 600000 g/mol, preferably from 20000 to 400000 g/mol, more preferably from 30000 to 300000 g/mol, even more preferably from 40000 to 200000 g/mol, particularly preferably from 50000 to 100000 g/mol. In preferred embodiments, the peptide chains have a molecular weight of from 150 to 600000 g/mol, preferably from 200 to 400000 g/mol, more preferably from 300 to 300000 g/mol, more preferably from 400 to 200000 g/mol, more preferably from 500 to 100000 g/mol, even more preferably from 600 to 50000 g/mol, even more preferably from 700 to 10000 g/mol, particularly preferably from 750 to 5000 g/mol, for example from 800 to 1500 g/mol. In preferred embodiments, the peptide chains have a molecular weight of from 150 to 10000 g/mol, preferably from 300 to 5000 g/mol, more preferably from 500 to 4000 g/mol, even more preferably from 600 to 3000 g/mol, particularly preferably from 700 to 2000 g/mol, for example from 800 to 1500 g/mol. In preferred embodiments, the peptide chains have a molecular weight of from 10000 to 600000 g/mol, preferably from 20000 to 400000 g/mol, more preferably from 30000 to 300000 g/mol, even more preferably from 40000 to 200000 g/mol, particularly preferably from 50000 to 100000 g/mol. The peptides used in the present invention may be commercially available, or they may be described in the literature, or they may be produced biotechnologically, or they may be prepared according to methods known in the art. For example, the peptides used in the present invention may be prepared by solid phase peptide synthesis or by solution phase peptide synthesis. In general, peptides are prepared from the corresponding amino acids using known techniques (e.g. carboxylic acid activation, coupling reagents) and protecting group strategies. For example, the peptides used in the present invention, e.g. P1 to P5, can be prepared according to methods described in Gačanin, J. et al., Adv. Mater.2019, 31, 1805044 (Autonomous Ultrafast Self-Healing Hydrogels by pH-Responsive Functional Nanofiber Gelators as Cell Matrices). In one preferred embodiment, the peptide chains are of synthetic origin. In one preferred embodiment, the peptide chains are of natural origin. In preferred embodiments, the peptide chains are linked to the polysaccharide polymer through a linker. Any linker can be used. In a preferred embodiment, the linker results from the incorporation of a compound having at least two electrophilic functional groups. Preferably, the compound having at least two electrophilic functional groups has from 1 to 20 carbon atoms and from 0 to 10 heteroatoms, more preferably from 2 to 12 carbon atoms and from 1 to 7 heteroatoms, even more preferably from 3 to 9 carbon atoms and from 2 to 5 heteroatoms, particularly preferably from 4 to 7 carbon atoms and from 3 to 4 heteroatoms. Preferably, the at least two electrophilic functional groups are selected from epoxy groups, C=C double bonds, carbonyl groups, C=C double bonds substituted with at least one carbonyl group, and mixtures thereof. Preferably, the compound having at least two electrophilic functional groups is selected from glycidyl methacrylate, maleimide, and mixtures thereof. Particularly preferably, the compound having at least two electrophilic functional groups is glycidyl methacrylate. In one embodiment, the linker does not result from the incorporation of glycidyl methacrylate. In one embodiment, the hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b) peptide chains and (c) optionally a linker. Preferably, the combined amount of (a) the polysaccharide polymer and (b) the peptide chains and (c) optionally the linker in the hybrid polymer is at least 50 wt-%, more preferably at least 60 wt-%, more preferably at least 70 wt-%, more preferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably at least 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least 95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt-%, particularly preferably at least 99 wt-%, based on the total weight of the hybrid polymer. In one embodiment, the hybrid polymer of the invention comprises (a) a polysaccharide polymer and (b) peptide chains and (c) a linker. Preferably, the combined amount of (a) the polysaccharide polymer and (b) the peptide chains and (c) the linker in the hybrid polymer is at least 50 wt-%, more preferably at least 60 wt- %, more preferably at least 70 wt-%, more preferably at least 75 wt-%, more preferably at least 80 wt-%, more preferably at least 85 wt-%, even more preferably at least 90 wt-%, even more preferably at least 95 wt-%, even more preferably at least 97 wt-%, even more preferably at least 98 wt-%, particularly preferably at least 99 wt-%, based on the total weight of the hybrid polymer. In preferred embodiments, from 1 to 100%, preferably from 3 to 50%, more preferably from 5 to 40%, even more preferably from 8 to 30%, particularly preferably from 10 to 25%, of the monosaccharide units of the polysaccharide polymer are modified with the peptide chains, optionally through a linker. Modification of the monosaccharide units / the polysaccharide polymer typically occurs via modifiable groups of the monosaccharide units / the polysaccharide polymer. Preferably, a modifiable group is a hydroxy group. A modifiable group may, for example, also be an amino group. In the case of dextran, the monosaccharide unit is a glucose unit, and the modifiable group is a hydroxy group. In preferred embodiments, the peptide chains are linked to the polysaccharide polymer, optionally through a linker, via the N-terminal amino acid or the C-terminal amino acid of the peptide chains. In preferred embodiments, the peptide chains are linked to the polysaccharide polymer, optionally through a linker, via the N-terminal amino acid of the peptide chains. In preferred embodiments, the peptide chains are linked to the polysaccharide polymer, optionally through a linker, via the C-terminal amino acid of the peptide chains. Any amino acid can be used as the N-terminal amino acid or the C-terminal amino acid of the peptide chains. In one embodiment, the N-terminal amino acid or the C- terminal amino acid of the peptide chains is cysteine. In one embodiment, the N- terminal amino acid of the peptide chains is cysteine. In one embodiment, the C- terminal amino acid of the peptide chains is cysteine. In one embodiment, the N-terminal amino acid of the peptide chains is not lysine. In one embodiment, the C-terminal amino acid of the peptide chains is not cysteine. In one embodiment, the C-terminal amino acid of the peptide chains is selected from hydrophobic amino acids. Preferably, the hydrophobic amino acids are selected from leucine, isoleucine, phenylalanine, valine, tyrosine, tryptophan, glycine, alanine, proline, and methionine. In one embodiment, the C-terminal amino acid of the peptide chains is selected from methionine and phenylalanine. The N-terminal amino acid of the peptide chains may optionally be capped, for example, it may optionally be acetylated. The N-terminal amino acid of the peptide chains may optionally be protected with a protecting group, for example a fluorenylmethoxycarbonyl (Fmoc) group. The N-terminal amino acid of the peptide chains may optionally be capped, for example, with a C3-C6 alkyl group. The C- terminal amino acid of the peptide chains may optionally be capped, for example, it may optionally be amidated. The present invention also relates to a blend comprising (a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50 to 60 wt-%, of a hybrid polymer of the present invention, based on the total weight of the blend; and (b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40 to 50 wt-%, of one or more polysaccharide polymers and/or one or more peptide chains, based on the total weight of the blend. Preferred hybrid polymers are described further above. In a preferred embodiment, the blend of the invention comprises (a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50 to 60 wt-%, of a hybrid polymer of the present invention, based on the total weight of the blend; and (b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40 to 50 wt-%, of one or more polysaccharide polymers, based on the total weight of the blend. Preferred polysaccharide polymers are described further above. Preferably, the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, chitosan, xanthan gum, fenugreek gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose, amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karaya gum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotium gum, gellan gum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin, derivatives thereof and mixtures thereof. More preferably, the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, starch, amylose, amylopectin, tamarind kernel gum, arabica gum, karaya gum, konjac gum, pectin, sclerotium gum, gellan gum, diutan gum, inulin, derivatives thereof and mixtures thereof. Even more preferably, the polysaccharide polymer is selected from dextran, dextrin, xanthan gum, tara gum, locust bean gum, carrageenan, guar gum, starch, amylose, amylopectin, konjac gum, inulin, derivatives thereof and mixtures thereof. Particularly preferably, the polysaccharide polymer is xanthan gum. In a preferred embodiment, the blend of the invention comprises (a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50 to 60 wt-%, of a hybrid polymer of the present invention, based on the total weight of the blend; and (b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40 to 50 wt-%, of one or more peptides, based on the total weight of the blend. Preferred peptides are described further above. The present invention also relates to the use of a hybrid polymer of the present invention or a blend of the present invention as a rheology modifying agent. In a preferred embodiment, the rheology modifying agent is a thickening agent. Preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a rheology modifying agent in a cosmetic formulation. In a preferred embodiment, the cosmetic formulation is a skin care formulation or a hair care formulation. More preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a rheology modifying agent in a skin care formulation or a hair care formulation. Particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a rheology modifying agent in a skin care formulation. Also particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a rheology modifying agent in a hair care formulation. Preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a cosmetic formulation. In a preferred embodiment, the cosmetic formulation is a skin care formulation or a hair care formulation. More preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a skin care formulation or a hair care formulation. Particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a skin care formulation. Also particularly preferably, the hybrid polymer of the present invention or the blend of the present invention is used as a thickening agent in a hair care formulation. The present invention also relates to a hydrogel comprising a hybrid polymer of the present invention or a blend of the present invention, water, optionally a pH adjusting agent, and optionally an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, and a pH adjusting agent or an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, and a pH adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, and an ionic strength adjusting agent. In one embodiment, the hydrogel comprises a hybrid polymer of the present invention or a blend of the present invention, water, a pH adjusting agent, and an ionic strength adjusting agent. Preferred hybrid polymers are described further above. In preferred embodiments, the hydrogel comprises from 0.1 to 10 wt-%, preferably from 0.2 to 5 wt-%, more preferably from 0.3 to 3 wt-%, even more preferably from 0.4 to 2 wt-%, particularly preferably from 0.5 to 1 wt-%, of the hybrid polymer or the blend, based on the total weight of the hydrogel. Preferably, the hydrogel comprises a pH adjusting agent. The pH adjusting agent may, for example, be an acid, a base, a buffer, or combinations thereof. Examples of preferred acids are hydrochloric acid, acetic acid, trifluoroacetic acid, citric acid, formic acid, vitamin C, or combinations thereof. Examples of preferred bases are sodium hydroxide, potassium hydroxide, sodium carbonate, potassium carbonate, sodium bicarbonate (sodium hydrogencarbonate), potassium bicarbonate (potassium hydrogencarbonate), or combinations thereof. Examples of preferred buffers are phosphate buffer, citrate buffer, acetate buffer, or combinations thereof. A particularly preferred pH adjusting agent is a buffer. A particularly preferred buffer is a phosphate buffer. A particularly preferred pH adjusting agent is a phosphate buffer. Optionally, the hydrogel comprises an ionic strength adjusting agent. The ionic strength adjusting agent may, for example, be a salt. Examples of preferred salts are sodium chloride, potassium chloride, or combinations thereof. A particularly preferred ionic strength adjusting agent is sodium chloride. Preferably, the hydrogel has a pH of from 3 to 9, more preferably from 4 to 8.5, even more preferably from 5 to 8, particularly preferably from 5.5 to 7.5. In preferred embodiments, the hydrogel further comprises an active ingredient. Preferably, the active ingredient is selected from vitamins, moisturizing agents, anti- aging agents, anti-wrinkle agents, anti-inflammatory agents, amino acids, peptides, and mixtures thereof. More preferably, the active ingredient is selected from vitamins, moisturizing agents, anti-aging agents, anti-wrinkle agents, anti-inflammatory agents, and mixtures thereof. The present invention also relates to a formulation comprising (a) from 0.1 to 10 wt-%, preferably from 0.2 to 5 wt-%, more preferably from 0.3 to 3 wt-%, even more preferably from 0.4 to 2 wt-%, particularly preferably from 0.5 to 1 wt-%, of a hybrid polymer of the present invention or a blend of the present invention, based on the total weight of the formulation; and (b) from 90 to 99.9 wt-%, preferably from 95 to 99.8 wt-%, more preferably from 97 to 99.7 wt-%, even more preferably from 98 to 99.6 wt-%, particularly preferably from 99 to 99.5 wt-%, of one or more further components, based on the total weight of the formulation. In a preferred embodiment, the formulation is a cosmetic formulation, preferably a skin care formulation or a hair care formulation. In one preferred embodiment, the formulation is a skin care formulation. In another preferred embodiment, the formulation is a hair care formulation. In preferred embodiments, the formulation is selected from the group consisting of shampoo, body wash, facial cleanser, face mask, bubble bath, intimate wash, bath oil, cleansing milk, micellar water, make-up remover, cleansing wipes, hair mask, perfume, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti- aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin-whitening gel, self-tanning cream, anti-acne gel, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, eyeliner, night cream, eye brow gel, highlighter, lip stain, hand sanitizer, hair oil, nail varnish remover, skin conditioner, hair conditioner, hair styling gel, hair styling cream, anti- frizz serum, scalp treatment, hair colorant, split end fluid, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, bar soap, cuticle cream, lip balm, hair treatment, eye shadow, bath additive, body mist, eau de toilette, mouthwash, toothpaste, lubricating gel, moisturizer, serum, toner, aqua sorbet, cream gel, styling mousse, dry shampoo, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, hair spray, combing cream, and sunblock. In more preferred embodiments, the formulation is selected from the group consisting of body wash, facial cleanser, face mask, bubble bath, intimate wash, bath oil, cleansing milk, micellar water, make-up remover, cleansing wipes, perfume, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti-aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin- whitening gel, self-tanning cream, anti-acne gel, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, eyeliner, night cream, eye brow gel, highlighter, lip stain, hand sanitizer, nail varnish remover, skin conditioner, scalp treatment, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, bar soap, cuticle cream, lip balm, eye shadow, bath additive, body mist, eau de toilette, mouthwash, toothpaste, lubricating gel, moisturizer, serum, toner, aqua sorbet, cream gel, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, and sunblock. In even more preferred embodiments, the formulation is selected from the group consisting of body wash, facial cleanser, face mask, intimate wash, cleansing milk, micellar water, make-up remover, cleansing wipes, liquid soap, shaving soap, shaving foam, cleansing foam, day cream, anti-aging cream, body milk, body lotion, body mousse, face serum, eye cream, sunscreen lotion, sun cream, face cream, after-shave lotion, pre-shaving cream, depilatory cream, skin-whitening gel, self- tanning cream, mascara, foundation, primer, concealer, blush, bronzer, blemish balm (bb) cream, night cream, highlighter, lip stain, hand sanitizer, nail varnish remover, skin conditioner, deodorant, antiperspirant, baby cream, insect repellent, hand cream, sunscreen gel, foot cream, exfoliator, body scrub, cellulite treatment, cuticle cream, lip balm, lubricating gel, moisturizer, toner, cream gel, lip stick, lip gloss, body oil, shower milk, illuminator, lip crayon, and sunblock. The following examples are intended to illustrate the subject-matter of the present invention without restricting it thereto. Examples P1 – P5 refer to peptides (P1 – P3) and depsi peptides (P4 – P5). P1 was formed from depsi peptide P4 upon increasing the pH to neutral. P2 was formed from depsi peptide P5 upon increasing the pH to neutral. In addition, P1 and P2 can be synthesized directly, e.g., via solid phase peptide synthesis, without intermediate depsi peptide stage. All used amino acids are L-amino acids. P1 – P5 were prepared according to methods known in the art. If not stated otherwise, RT refers to room temperature (20 – 25°C). 1 Synthesis 1.1 Dextran-methacrylate (1a, 1b, 2): Glycidyl methacrylate (GMA, 3) functionalization of dextran (4, 5) In a typical reaction, dextran (15 g, molecular weight (MW) 40,000 g/mol, 4), provided in a flask in nitrogen atmosphere, was dissolved by addition of dry dimethyl sulfoxide (DMSO, 90 mL) and stirred (approx.30min) until dissolution was complete. The mixture was heated to 40°C under stirring in an oil bath to help with dissolution. 4- (Dimethylamino)pyridin (DMAP, 2.25g, 0.2eq, 6) was dissolved in dry DMSO (24 mL) separately. Subsequently, GMA (4.65 mL, 0.4 eq, 3) was added to the DMAP (6) solution and the mixture was added to the dextran solution. The reaction was stirred 20 h at 40°C. All steps were performed under nitrogen atmosphere. The reaction was purified by dialysis (molecular weight cut-off (MWCO) 3.5 kDa) in deionized water for 5 days including water exchange every 2-3 h on day one and twice a day the remaining time. After lyophilization for 4 days, the product (1a) was obtained as white solid. The quantification of GMA functionalization was conducted via ¹H NMR (DMSO-d₆). The reaction resulted in the modification of ~21% glucose units in dextran with methacrylate functional groups. The described method was applied to dextran of various molecular weights, e.g., MW 40 kg/mol (4) and 150 kg/mol (5), resulting in their methacrylated species, i.e., 1a, 1b, or 2, respectively. Variations of different molecular weights of dextran and different degrees of methacrylation were achieved by varying the educts as summarized in Table 1. Table 1: Overview of dextran GMA-functionalization syntheses.1a, 1b: Dextran-GMA from Dextran 40 kg/mol.2: Dextran-GMA from Dextran 150 kg/mol. GMA (3): glycidyl methacrylate. DMAP (6): 4-(Dimethylamino)pyridin. Dextran- Dextran DMSO GMA DMAP Reaction Functionali- GMA (3) (6) zation ratea m (g) V (mL) V (mL) m (g) Time (h) GMA^b (%) 1a 4 15 114 4.65 2.25 20 21 1b 4 1 10 0.31 0.15 20 13 2 5 1 10 0.31 0.15 20 19 ^a analyzed via 1H NMR ^b % of glucose repeating units modified with GMA 1.2 Peptide-dextran Hybrids General synthesis description, exemplary for hybrid H1 on the basis of peptide P4 (CKIKI*SQINM, the asterix (*) implies the position of the ester bond within the depsi peptide, C: Cysteine, K: Lysine, I: Isoleucine, S: Serine, Q: Glutamine, N: Asparagine, M: Methionine): The GMA-functionalized dextran (1, 40kDa, 10 mg) was dissolved in 0.1% trifluoracetic acid (7, TFA) in water (MilliQ, 0.2mL) (A). Separately, tris-(2-carboxyethyl)-phosphin (8, TCEP, 2.4 mg, 0.15 eq) was dissolved in 0.1% TFA/H2O (0.3 mL) and added to the peptide (P4, 21.0 mg, 0.3 eq.), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H₂O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 4000 rpm, 25°C. After lyophilization for 3 days, the hybrid (H1) was obtained as white powder. For larger batch sizes, lyophilization times were extended. The used amounts of biopolymer, peptide, TCEP and solvent were varied to achieve various functionalization efficiencies as demonstrated in Table 2. Table 2: Overview of peptide-hybrid syntheses.1a,b: Dextran-GMA from dextran 40 kg/mol.2: Dextran-GMA from dextran 150 kg/mol. GMA: glycidyl methacrylate. TCEP (8): tris-(2-carboxyethyl)-phosphin. P4: CKIKI*SQINM, P5: CEIEI*SQINM, P3: CKFKFQF. (C: Cysteine, K: Lysine, I: Isoleucine, S: Serine, Q: Glutamine, N: Asparagine, M: Methionine, E: Glutamic acid, F: Phenyl alanine). Hybrid Dextran- Peptide TCEP Functionalization ratea GMA m m m GMA b Educt GMA Peptide^c (mg) (mg) (mg) (%) conversion (%) (%) H1 1b 10 P4 21 2.4 13 100 13 H2 1b P5 H3 1b 10 P3 22 2.4 13 100 13 H4 1a 100 P4 92 25 21 H5 1a 500 P4 920 243.5 21 93 20 H6 1a 1000 P4 1840 495.2 21 85 18 H7 2 10 P4 5 2.4 19 H8 2 10 P4 10 2.4 19 89 17 H9 2 10 P4 20 2.4 19 100 19 H10 2 100 P4 184 49 19 H11 2 100 P4 92 25 19 ^a analyzed via 1H NMR ^b % of glucose repeating units modified with GMA ^c % of glucose repeating units modified with peptide 1.3 Hydrogel preparation a) Peptide-dextran hybrids i) Direct addition of buffer to hybrid (solid): The hydrogel was prepared by direct addition of the respective amount of buffer to the hybrid powder. For example, to obtain a 1wt% hydrogel, 30 µL of 100mM phosphate buffer pH 7.4 were added to 0.3 mg hybrid. Gelation occurred upon gentle mixing. ii) pH switch of pre-dissolved hybrid (acidic solution): Preferably, the hydrogel was obtained by pre-dissolving the hybrid in acidic solution and adjusting pH to approximately pH 7. For example, to obtain a 1wt% hydrogel, 0.3 mg hybrid was dissolved in 15 µL 0.1%TFA/H2O (pH 2). Subsequently, gelation was initiated upon addition of 15 µL 300 mM phosphate buffer pH 9 to adjust the pH to neutral (pH 7). No further mixing or stirring was required. Addition in reverse order was also possible. Alternatively, 0.8 mg hybrid was dissolved in 20 µL 0.1%TFA/H2O (pH 2) and gelation was initiated upon addition of 60 µL 300 mM phosphate buffer pH 9 to adjust the pH to neutral. iii) Optimized pH switch of pre-dissolved hybrid (acidic solution): Most preferably, the hydrogel was obtained by pre-dissolving the hybrid in acidic solution as explained in ii), followed by incubation at approx. 55°C (50 – 60°C) for approximately 30-45 min. Subsequently, the pH was adjusted to approximately pH 7 by adding buffer, which was pre-heated to the same temperature as the hybrid, i.e., 55°C. For example, to obtain a 1wt% hydrogel, 20 mg hybrid was dissolved in 1 mL 0.1%TFA/H2O (pH 2) and heated to 55°C for 30-45 min. Subsequently, gelation was initiated upon addition of 1 mL 300 mM phosphate buffer pH 9 (55°C) to adjust the pH to neutral. No further mixing or stirring was required. iv) Variation of iii) for incorporation of preservatives: Optimized pH switch of pre- dissolved hybrid (acidic solution) with gel preservation: The hydrogel was obtained by pre-dissolving the hybrid in acidic solution as explained in iii). Subsequently, the pH was adjusted to approximately pH 7 by adding buffer, which was pre-heated to the same temperature as the hybrid, i.e., 55°C. The buffer was supplemented with preservative (e.g., Nipaguard DMDMH Plus, 0.6 w%). For example, to obtain a 1wt% hydrogel, 30 mg hybrid was dissolved in 1.5 mL 0.1%TFA/H2O (pH 2) and heated to 55°C for 30-45 min. Subsequently, gelation was initiated upon addition of 1.5 mL 300 mM phosphate buffer pH 9 supplemented with Nipaguard DMDMH Plus (0.6w%, 7.8µL) (55°C) to adjust the pH to neutral. No further mixing or stirring was required. v) Use of an alternative buffer for adjustment of pH to neutral is possible. For example, instead of 300 mM phosphate buffer pH 9, 300 mM phosphate buffer pH 7 could be used to switch the pH from acidic to neutral. Similarly, other acids, e.g., vitamin C, could be used to dissolve the hybrids at pH 2. b) Composite hydrogels of peptide-dextran hybrids and polysaccharides i. Xanthan gum: Optimized pH switch The hydrogel was obtained by pre-dissolving the hybrid in acidic solution, followed by incubation at 55°C (50°C-60°C) for 30-45min (see 1.3aiii). To prepare the composite hydrogel, Xanthan gum (X.gum) hydrogel was added. Subsequently, the pH was adjusted to approximately pH 7 by adding phosphate buffer. For example, to obtain a 0.8wt% composite hydrogel (see Table 3: 1), 10 mg hybrid was dissolved in 1 mL 0.1%TFA/H2O (pH 2) and heated to 55°C for 30-45 min. Next, 1 mL of 1wt% X.gum hydrogel was added to the solution and well mixed. Subsequently, gelation of the hybrid was initiated upon addition of 0.5 mL 300 mM phosphate buffer pH 9 to adjust the pH to neutral. No further mixing or stirring was required. The most preferable hybrid to X.gum ratio was 1:1 (weight ratio). However, alternative ratios could be chosen to adjust the gel properties as summarized in Table 3. Table 3: Exemplary summary of different composite hydrogel preparations via peptide- dextran hybrids and other polysaccharides. Variation of different factors allowed for precise tailoring of the material properties. Amongst these are the final gel weight percentage (wt%), the peptide-dextran hybrid (H) and its weight percentage (H wt% indicates the used percentage), the composite polysaccharide (e.g., X.gum: Xanthan gum, 9) and its weight percentage (X.gum wt% indicates the percentage of the added X.gum hydrogel), and the mixing ratios. VolH and VX.gum: Volume used to dissolve the hybrid or X.gum, respectively. TH and TX.gum: Temperature at which the hybrid or X.gum was dissolved, respectively. Vbuffer: Volume of buffer that was added. R: Weight ratio of hybrid to X.gum. H H Vol_H T_H X.gum X.gum V_X.gum T_X.gum V_buffer R Gel wt% (mL) (°C) wt% solvent (ml) (°C) (mL) wt% 1 H5/ 1 1 55 1 water 1 RT 0.5 1:1 0.8 H6 2 H5/ 2 1 55 2 water 1 RT 0.5 1:1 1.6 H6 3 H4/ 1 1 55 2 water 1 RT 0.5 1:2 1.2 H7 4 H4/ 2 1 55 1 water 1 RT 0.5 2:1 1.2 H5/ H6/ H7 5 H5 0.4 1 55 2 water 1 RT 0.5 1:5 1 6 H5 2 1 55 0.4 water 1 RT 0.5 5:1 1 7 H5 1 1 55 1 water 1 RT 0.5 1:1 0.8 8 H5 1 1 55 2 water 1 RT 0.5 1:2 1.2 9 H5 2 1 55 2 water 1 RT 0.5 1:1 1.6 10 H5 2 1 55 1 water 1 RT 0.5 2:1 1.2 11 H5 2 0.5 RT 2 0.1% 0.5 RT 1 1:1 1 TFA/ H₂O 12 H5 2 0.5 55 1 0.1% 0.5 55 1 2:1 0.75 TFA/ H2O ii. Dextran (1) Dextran (4, e.g., 10 mg or 20 mg) was dissolved together with the hybrid (20 mg) in 0.1% TFA/H2O (1mL total volume, pH 2), heated to 55°C, and 300 mM phosphate buffer pH 9 (1 mL) was added to adjust the pH to neutral. The procedure was performed according to 1.3aiii. (2) The hybrid (e.g., 10 mg or 20 mg) was dissolved in 0.1% TFA/H2O (1mL, pH 2), heated to 55°C, and dextran (20 mg) pre-dissolved in 300 mM phosphate buffer pH 9 (1 mL) was added to adjust the pH to neutral. The procedure is performed according to 1.3aiii. (3) Solution A was prepared by adding 0.1%TFA/H₂O (7.5 µL) to H1 (0.15mg). Solution B was prepared by adding 0.1%TFA/H2O (7.5 µL) to dextran (4, 0.15mg). Next, solution B was introduced to solution A with mixing. Subsequently, phosphate buffer (15 µL, 300mM, pH 9) was added with mixing. The procedure was performed according to 1.3aii. iii. Hyaluronic acid The hydrogel was obtained by pre-dissolving the hybrid in acidic solution, followed by incubation at 55°C (50°C-60°C) for 30-45min (see 1.3aiii). To prepare the composite hydrogel, hyaluronic acid was added. Subsequently, the pH was adjusted to approximately pH 7 by adding phosphate buffer. For example, to obtain a composite hydrogel, 10 mg hybrid H6 was dissolved in 1 mL 0.1%TFA/H2O (pH 2) and heated to 55°C for 30-45 min. Next, 1 mL of pre-dissolved hyaluronic acid (10mg, H₂O) was added to the solution and mixed well. Subsequently, gelation of the hybrid was initiated upon addition of 0.5 mL 300 mM phosphate buffer pH 9 to adjust the pH to neutral. No further mixing or stirring is required. 2 Methods / Characterizations 2.1 NMR ¹H NMR was conducted to quantify functionalization rates of polysaccharides with GMA or peptides. DMSO-d₆ was used for analysis. Spectra were recorded on a Bruker 300 MHz or 400 MHz NMR spectrometers. 2.2 Rheology Rheological characterization of hydrogels and formulations was conducted using a DHR3 rheometer (TA Instruments) equipped with a temperature controller. Experiments were performed using a) 8 mm parallel-plate geometry with solvent reservoir to prevent hydrogel drying with hydrogels of 30 μL volume resulting in a gap size of ~ 0.50 mm, or b) 20 mm cone-plate geometry (2.007°) with solvent reservoir to prevent hydrogel drying, or c) 40 mm cone-plate geometry. In general, characterization of the mechanical properties was performed at 20 °C. In addition, the mechanical properties at temperatures between 5 °C to 60 °C were analyzed as well. Several different measurement setups were performed: (i) Time sweep: The linear viscoelastic region was found to include the range of 0.05 – 1% strain and 1 – 1.6 Hz frequency. Therefore, oscillatory time-sweep measurements were performed at a fixed strain and fixed frequency within this range at different temperatures and time intervals. (ii) Strain sweep 1: Oscillatory strain sweeps were conducted for strains between 0.01 – 1000% at a fixed frequency of 1 Hz at 25 °C or as indicated. (iii) Strain sweep 2: Oscillatory strain sweeps were conducted for strains between 0.1 – 100% at a fixed frequency of 1 Hz at 20 °C. (iv) Thixotropy measurement 1: Consecutive combined measurements of an oscillatory strain sweep (0.01 – 1000%) at 25°C with a fixed frequency of 1 Hz followed by an oscillatory time sweep measurement with a fixed strain of 0.1% and frequency of 1 Hz for 800 s or 1000 s at 25 °C were conducted to analyze the self-healing capacity of the hydrogels. Notably, the healing efficiency of hydrogels and formulations was quantified from the storage modulus acquired from this experiment. In this context, the initial hydrogel recovery (first acquired data point, ~ 13 s) and the mean hydrogel recovery during the following oscillatory time sweep (0.1% strain, 800s) were analyzed for each strain sweep. (v) Thixotropy measurement 2: Consecutive combined measurements of an oscillatory strain sweep (0.01 – 100%) at 20°C with a fixed frequency of 1 Hz followed by an oscillatory time sweep measurement with a fixed strain of 0.1% and frequency of 1 Hz for 300 s were conducted to analyze the self-healing capacity of the hybrid X.gum composite hydrogels. Notably, the healing efficiency of hydrogels and formulations was quantified from the storage modulus acquired from this experiment. In this context, the mean hydrogel recovery during the following oscillatory time sweep (0.1% strain, 300s) were analyzed for each strain sweep. (vi) Rheological recovery test: Combined measurements of consecutive oscillatory time sweeps with alternating high strain (200%, 120 s) and low strain (0.1%, 120 s) at 20 °C with a fixed frequency of 1 Hz. Up to 10 repetitions were performed. (vii) Flow ramp: Continuous flow rheology experiment. Flow ramp from initial stress of 0 to up to 60 Pa over 180 s at 20 °C or 25 °C. (viii) Temperature sweep: Oscillatory temperature sweep measurements were performed at a fixed strain (0.05%) and fixed frequency (1 Hz). First, a temperature sweep with 5 °C start temperature and 60 °C end temperature was conducted, which was followed by the inverse temperature sweep from 60°C to 5°C; both measurements were conducted with temperature steps of 5°C. (ix) Temperature analysis: Consecutive measurement of oscillatory time sweep measurement (0.05% strain, 1 Hz, 2400s, 20°C); temperature sweep 20°C 60°C (start temperature 20°C and end temperature 60°C with temperature step 5°C, 0.05% strain, 1 Hz), inverse temperature sweep 60°C 20°C (start temperature 60°C and end temperature 20°C with temperature step 5°C, 0.05% strain, 1 Hz), time sweep (soaking time 180 s, 0.05% strain, 1 Hz, 400s, 20°C), thixotropy measurement (consecutive alternating oscillatory amplitude sweep 0.01% – 1000%, 1Hz and time sweep 0.05% strain, 1 Hz, 1000s; both at 20°C). In addition, several experiments were performed using these experimental setups: x) Investigation of peptide graft amino acid sequence effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (positively or negatively charged, or variation of hydrophobic amino acids to include aromatic residues) xi) Investigation of peptide grafting density effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (H1 – H8, e.g., 0% - 20% of glucose units per dextran molecule with peptide functionalization) xii) Investigation of polysaccharide backbone length effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (e.g., dextran 40 kg/mol or 150 kg/mol) xiii) Investigation of temperature effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (T 5°C – 60°C) xiv) Investigation of pH effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (pH 5 – pH 9) In order to assess the effect of pH changes on the hydrogel mechanical properties, hydrogels were prepared at pH 7 via pH switch as described before. Next, hydrogels were washed with buffer until the desired pH was reached and rheological characterization was conducted. For example, 1 wt% hydrogel was prepared by introducing 0.3mg H1 in 15 μL 0.1%TFA/H2O and inducing gelation by addition of 15 μL 300 mM phosphate buffer pH 9. Gelation was completed. After 10 min, the gel was washed with either 150mM phosphate buffer pH 7 for control, with acetate buffer 100 mM pH 4.75, or with phosphate buffer pH 9150 mM. xv) Investigation of salt effect on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (NaCl, 0 or 5 wt%) Moreover, in addition to hydrogels from peptide-dextran hybrids, several of the above-mentioned experiments were also performed with composite materials: xvi) Investigation of addition of peptides (not grafted) of different amino acid sequences on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery. Thereby, peptides were introduced as freshly prepared peptide solution in the pH 2 phase (monomers) or as pre-incubated fibrils in the pH 9 phase. xvii) Investigation of addition of free polysaccharide on gel mechanical properties like stiffness, crossover strain, thixotropy, recovery (dextran, xanthan gum) 2.3 Tilting / Overturn test in glass vial Hydrogels of 2.5 mL volume were prepared in small glass vials of 5 mL total volume according to preparation protocols described herein. Upon gelation, the glass vials were tilted by 180°C to demonstrate flow for liquids or weak gels/formulations or absence of flow for gels/formulations. 2.4 Incorporation of actives a) Vitamin C (10, 5wt% final concentration) i) Most preferably, H6 (10 mg) and vitamin C (125 mg) were dissolved in H2O (MilliQ, 0.5 mL), Xanthan gum (9, 1 wt% in water, 1 mL) was added under mixing. Subsequently, phosphate buffer (300 mM, pH 9, 2 mL) was added to the mixture to adjust pH to neutral. ii) H6 (10 mg) was dissolved in a vitamin C solution (125 mg in 0.1%TFA/H₂O, 1 mL). Xanthan gum (1 wt% in water, 1 mL) was added under mixing. Subsequently, phosphate buffer (300 mM, pH 9, 2 mL) was added to the mixture to adjust the pH to neutral. iii) H6 (10 mg) was dissolved in a vitamin C solution (125 mg in 0.1%TFA/H2O, 1 mL) and heated to about 55°C for 30min. Xanthan gum (1 wt% in water, 1 mL) was added under mixing. Subsequently, phosphate buffer (300 mM, pH 9, 2 mL) was added to the mixture to adjust the pH to neutral. b) Peptides i. Monomer Solution A was prepared by adding 0.1%TFA/H2O (7.5 µL) to H1 (0.15 mg). Solution B was prepared by adding 0.1%TFA/H₂O (7.5 µL) to P4 or P5 (0.15 mg), respectively. Next, solution B was introduced to solution A with mixing. Subsequently, phosphate buffer (15 µL, 300 mM, pH 9) was added with mixing. In the course of the pH switch, depsi peptides rearrange to their linear counterpart, i.e., P1 is formed from P4, while P2 is formed from P5 due to the switch, and aggregation is initiated. ii. Pre-assembled fibrils Solution A was prepared by adding 0.1%TFA/H₂O (7.5 µL) to H1 (0.15mg). Solution B was prepared by adding 0.1%TFA/H2O (7.5 µL) to P4 (0.15mg). Solution B was then introduced to phosphate buffer (15 µL, 300mM, pH 9) with mixing and incubated 5 min at RT without stirring or shaking. In the course of the pH switch, depsi peptides rearrange to their linear counterpart, i.e., P1 is formed from P4 due to the switch, and aggregation is initiated. Next, this mixture was introduced to solution A with mixing. 2.5 Cytoviability Cytoviability of hydrogels and components was evaluated by performance of a CellTiter-Glo® Luminescent Cell Viability Assay. The tests were carried out with extracts of hydrogels pre-incubated in cell medium in reference to DIN EN ISO 10993- 5 (Biologische Beurteilung von Medizinprodukten – Teil 5: Prüfungen auf In-vitro- Zytotoxizität). Extracts were prepared and cells were seeded on day -1: 1wt% hydrogels (H1 or H5/H6) were prepared according to 1.3ai or 1.3aii and left for gelation (15 min, RT). Cell medium (DMEM fully supplemented 1% Penicillin/Streptomycin, 1% non-essential amino acids (NEAA), 5% fetal bovine serum (FCS); 200 µL) was added. Soluble components (dextran 40 kg/mol (4), dextran-GMA (1), P4) were pre-dissolved similarly to the gelling hybrids in buffer according to 1.3ai or 1.3aii to yield 1wt% or 0.5wt% and cell medium was added (200 µL). For controls, cell medium was used as blind value (Blindwert), positive control was doxorubicin 500 µM (in cell medium), control was buffer (same concentration as in extract preparation: 20 µL buffer (100mM phosphate buffer pH 7.4) plus 200 µL cell medium), and cell medium was used as blank (without cells). The extracts, sample solutions, and controls were incubated overnight at 37°C. Additionally, cells were seeded according to the manufacturer’s protocol (half area plate, 5000 A549 cells per well (50 µL; 1x10^-5 cells/mL), fully supplemented DMEM) and incubated overnight (37°C, 5% CO2). On day 0, the cell medium was removed from the wells and replaced by extracts, samples in solution, or controls (50 µL per well), which were added to the cells (triplets) and incubated for 24h (37°C, 5% CO2). On day 1, the CellTiter-Glo® Luminescent Cell Viability Assay was performed according to manufacturer’s protocol. 2.6 Hydrogel degradation assays: Biodegradation The biodegradation study (Biological Oxygen Demand (BODn) Method) was performed according to OECD 301F. During the measurement, the BOD-Direct Plus System was situated in an incubator heated to 20°C. As standard, Na-Benzoate (50 mg/l) was used. Concentration of the test substance (H5) was ~50 mg/l. Tests were performed with an inoculum in a closed bottle for 28 days. 2.7 Hydrogel long-term temperature stability (macroscopic) Hydrogel (H6, 1 mL, 1wt%) was prepared in a glass vial according to 1.3aiv and incubated at 4°C, room temperature (approx.20°C), or 37°C. 2.8 Molecular weight The molecular weight of the polysaccharide polymer was determined using gel permeation chromatography (GPC). GPC experiments were performed using a PSS SECcurity² instrument consisting of a pump, autosampler and column oven. A column SUPREMA LIN XL (PSS Polymer Standards Service GmbH, Mainz, Germany) of 300 x 8 mm and 10 µm average particle size was used at a flow rate of 1.0 mL/min and a column temperature of 25°C. As eluent 0.1M NaNO₃ was used. The samples having 1 mg/ml concentration were filtered prior to measurement through 0.45 µm HA filter. The injection volume was 50 μL. Detection was accomplished with an RI detector. Data acquisition and evaluation were performed using PSS WINGPC UniChrom (PSS Polymer Standards Service GmbH, Mainz, Germany). Calibration was carried out by using dextran standards (molecular weight ranging from 298000 g/mol to 180 g/mol) (PSS Polymer Standards Service GmbH, Mainz, Germany). In general, calibration is carried out by using an appropriate standard. A person skilled in the art knows how to select an appropriate standard. In the experimental section of the present patent application, reference is made to “Dextran 40 kg/mol”, “dextran (… molecular weight (MW) 40,000 g/mol, 4)”, “dextran ... MW 40 kg/mol (4)”, “Dextran 4”, or variations thereof. This dextran is commercially available, and its packaging indicates a molecular weight of 40 kg/mol (determined by intrinsic viscosity). However, when the molecular weight of this dextran is determined according to the method described herein (chapter 2.8), i.e. using gel permeation chromatography (GPC) as described herein (chapter 2.8), the following results are obtained: Mn = 15099 g/mol, Mw = 33693 g/mol. In the experimental section of the present patent application, reference is made to “Dextran 150 kg/mol”, “dextran … MW 150 kg/mol (5)”, “Dextran 5”, or variations thereof. This dextran is commercially available, and its packaging indicates a molecular weight of 150 kg/mol (determined by intrinsic viscosity). However, when the molecular weight of this dextran is determined according to the method described herein (chapter 2.8), i.e. using gel permeation chromatography (GPC) as described herein (chapter 2.8), the following results are obtained: Mn = 20312 g/mol, Mw = 156959 g/mol. A bimodal distribution of molecular weight was observed. 3 Formulations 3.1 Volume: 5 mL Table 4: Cream - Formulation No.1. Substance Amount Solvent A Plantasens Emulsifier HE20 150 mg n/a (Cetearyl Glucoside & Sorbitan Olivate) Myritol 318 500 mg n/a (Caprylic/Capric Triglyceride) B H5 20 mg 0.1%TFA in H2O (1.12 mL) C Xanthan gum 1wt%, 2mL^a H2O Glycerin (85%) 150 mg n/a Nipaguard DMDMH Plus 30 mg n/a (DMDM Hydantoin) D Phosphate buffer (pH 9) 300 mM H2O (1 mL) ^a 2 mL of a pre-dissolved 1wt% X.gum hydrogel, this specification equals 20 mg X.gum in 2 mL water. Procedure: I) Dissolve B at about 55°C for 30 min. II) Melt A at about 80°C. III) Heat C to 80°C. IV) Add III) into II) under stirring and emulsify (above water bath). V) Add IV) to I) under stirring. VI) Add D to V) under gentle stirring. VII) Allow cooling down without stirring. Table 5: Cream - Formulation No.2. Substance Amount Solvent A Plantasens Emulsifier HE20 150 mg n/a (Cetearyl Glucoside & Sorbitan Olivate) Myritol 318 500 mg n/a (Caprylic/Capric Triglyceride) B H5 10 mg 0.1%TFA in H2O (1.12 mL) C Xanthan gum 2wt%, 2mL^a H2O Glycerin (85%) 150 mg n/a Nipaguard DMDMH Plus 30 mg n/a (DMDM Hydantoin) D Phosphate buffer (pH 9) 300 mM H2O (1 mL) ^a 2 mL of a pre-dissolved 2wt% X.gum hydrogel, this specification equals 40 mg X.gum in 2 mL water. Procedure: I) Dissolve B at about 55°C for 30 min. II) Melt A at about 80°C. III) Heat C to 55°C for 30 min. IV) Add III) into I) under stirring and emulsify (above water bath). V) Add II) to IV) under stirring. VI) Add D to V) under stirring. VII) Allow cooling down without stirring. Table 6: Cream - Formulation No.3. Substance Amount Solvent A Plantasens Emulsifier HE20 150 mg n/a (Cetearyl Glucoside & Sorbitan Olivate) Myritol 318 500 mg n/a (Caprylic/Capric Triglyceride) B H5 40 mg 0.1%TFA in H₂O (1.12 mL) C Xanthan gum 0.4wt%, H₂O 2mL^a Glycerin (85%) 150 mg n/a Nipaguard DMDMH Plus 30 mg n/a (DMDM Hydantoin) D Phosphate buffer (pH 9) 300 mM H2O (1 mL) ^a 2 mL of a pre-dissolved 0.4wt% X.gum hydrogel, this specification equals 8 mg X.gum in 2 mL water. Procedure: I) Dissolve B at about 55°C for 30 min. II) Melt A at about 80°C. III) Heat C to 80°C. IV) Add III) into II) under stirring and emulsify (above water bath). V) Add IV) to I) under stirring. VI) Add D to V) under gentle stirring. VII) Allow cooling down without stirring. 3.2 Volume: 25 mL Table 7: Cream - Formulation No.4. Substance Amount Solvent A Plantasens Emulsifier HE20 750 mg n/a (Cetearyl Glucoside & Sorbitan Olivate) Myritol 318 2500 mg n/a (Caprylic/Capric Triglyceride) B H6 100 mg 0.1%TFA in H2O (5.6 mL) C Xanthan gum 1wt%, H2O 10mL^a Glycerin (85%) 750 mg n/a D Phosphate buffer (pH 9) 300 mM H2O (5 mL) E Nipaguard DMDMH Plus 150 mg n/a (DMDM Hydantoin) ^a 10 mL of a pre-dissolved 1wt% X.gum hydrogel, this specification equals 100 mg X.gum in 10 mL water. Procedure: I) Dissolve B at about 55°C for 60min. II) Melt A at about 80°C. III) Heat C to 80°C. IV) Stir III) into II) and homogenize with a high sheer mixer at 16000 rpm. V) Allow cooling down to about 20°C while stirring with magnetic stirrer. VI) Add V) to I) under stirring. VII) Add D to V) under stirring. VIII) Add E under stirring. IX) Allow cooling down without stirring. 4 Results 4.1 NMR (GMA functionalization and peptide conjugation) Polysaccharides, i.e. dextran, of different molecular weights were functionalized to a varying extent with GMA to yield a biopolymer platform for further peptide conjugation. Analysis via 1H NMR with DMSO-d6 as solvent was used to determine the degree of GMA-modification of the polymers. The results are summarized in Table 1 and refer to the percentage of GMA-functionalized repeat units, i.e. glucose units in the case of dextran. Calculations are based on the integrals of vinyl-signals of the GMA (approx.5.5-6.5 ppm) that was coupled to the biopolymer in relation to the integral of the proton signals of the glucose repeat units (approx.4-5 ppm). The degree of functionalization of dextran-GMA with peptides was calculated from the reduction in the integral of the vinyl signal (appr.5.5 - 6.5 ppm) in the hybrid. The results are summarized in Table 2. 4.2 Rheology 4.2.1 Peptide-dextran hybrids A) Adjustability of G’ Peptide-dextran hybrids resulted in hydrogels that featured an adjustability of G‘ via the type of grafted peptide, number of peptide grafts, i.e., peptide functionalization rate, and the wt% of the respective peptide-dextran hybrid. This was demonstrated with different peptide grafts on a polysaccharide, i.e., dextran backbone. i) 40 kg/mol dextran backbone Table 8: Adjustability of mechanical properties of hydrogels in dependency of peptide graft type, peptide functionalization rate, or wt% of hybrid. Unlike the hybrids, the plain backbone 1 was not capable of hydrogel formation or rheology modification. Using the hybrids, G’ was adjustable in a broad range. n.d. = not determined. Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. YP = Yield point. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M1: 1.3ai, 2.2b (cone plate), 2.2i, 0.05% strain, 10 rad/s, 25°C. M2: 1.3ai, 2.2b (cone plate), 2.2vii, 0-20Pa stress in 180s, 25°C. M3: 1.3ai, 2.2b (cone plate), 2.2vii, 0-50Pa stress in 180s, 25°C. M4: 1.3ai, 2.2a (parallel plate), 2.2i, 0.05% strain, 10 rad/s, 25°C. Compound FR (%) wt% G’ (Pa) G’’ (Pa) YP (Pa) 1 0 1 2 ^M1 1^M1 0 ^M2 H1 13 0.25 366 ^M1 48 ^M1 2 ^M2 H1 13 0.5 1457 ^M1 149 ^M1 14 ^M3 H1 13 1 4235 ^M4 455 ^M4 n.d. H1 13 4 42070 ^M4 4239 ^M4 n.d. H3 13 1.4 3695 ^M1 391 ^M1 n.d. H3 13 4 9837 ^M4 1104 ^M4 n.d. ii) 150 kg/mol dextran backbone Table 9: Adjustability of mechanical properties of hydrogels in dependency of peptide functionalization rate. Unlike the hybrids, the plain backbone 1 was not capable of hydrogel formation or rheology modification. n.d. = not determined. Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. YP = Yield point. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M1: 1.3ai, 2.2b (cone plate), 2.2i, 0.05% strain, 10 rad/s, 25°C. M2: 1.3ai, 2.2b (cone plate), 2.2vii, 0-20Pa stress in 180s, 25°C. M5: 1.3aii, 2.2a (parallel plate), 2.2i, 0.05% strain, 10 rad/s, 25°C. M6: 1.3aii, 2.2a (parallel plate), 2.2vii, 0-60Pa stress in 180s, 25°C. M7: 1.3aii, 2.2a (parallel plate), 2.2vii, 0-40Pa stress in 180s, 25°C. Compound FR (%) wt% G’ (Pa) G’’ (Pa) YP (Pa) 1 0 1 2 ^M1 1 ^M1 0 ^M2 H7 17 1 2997 ^M5 235 ^M5 15 ^M6 H8 17 1 3507 ^M5 310 ^M5 21 ^M6 H9 19 1 5288 ^M5 440 ^M5 26 ^M7 B) Self-healing behavior of 1wt% peptide-dextran hybrid hydrogels, demonstrated with peptide grafts on 40 kg/mol or 150 kg/mol dextran backbone (H1, H9) Table 10: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.a and R.b describe G’ regeneration after 13s or 1000s after the liquefying strain was removed, respectively. CS = Crossover strain with gel to sol transition (G’ = G’’). G’1 - G’4 give G’ after a regeneration time of 1000s in cycle 1-4, respectively. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M8: 1.3ai, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. M9: 1.3aii, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. Compound Initial Cycle 1 Cycle 2 FR G’i G’’i CS R.a R.b G’1 G’’1 CS R.a R.b G’2 G’’2 (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1^M8 13 2605 279 7 46 64 1671 166 6 53 85 1419 139 H1^M9 13 5161 526 21 24 26 1365 130 2 76 74 1014 79 H9 ^M9 19 5044 456 10 27 29 1443 134 2 75 70 1006 94 Cycle 3 Cycle 4 CS R.a R.b G’3 G’’3 CS R.a R.b G’4 G’’4 (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1^M8 5 66 98 1386 130 5 67 92 1279 117 H1^M9 3 85 89 900 69 3 76 88 794 57 H9 ^M9 n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. Both hybrid hydrogels from H1 and H9 showed regenerative behavior after mechanical stress. C) pH stability of peptide-dextran hybrid hydrogels and regeneration behavior (40 kg/mol dextran backbone with peptide grafts, 1wt% hydrogels) Table 11: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’i gives the G’ before liquefying strain was applied at 0.1% strain. CS = Crossover strain with gel to sol transition (G’ = G’’). R.a and R.b describe G’ regeneration after 13s or 1000s after the liquefying strain was removed, respectively. G’¹ - G’⁴ give G’ after a regeneration time of 1000s in cycle 1-4, respectively. Preparation of gels and rheology method for these experiments are given in chapter 2.2xiv. Measurement was performed with parameters correlating to M9: 1.3aii, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. H1 Initial Cycle 1 Cycle 2 pH FR G’_i G’’_i CS R._a R._b G’₁ G’’₁ CS R._a R._b G’₂ G’’₂ (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) 5 13 2053 154 30 24 37 767 49 5 56 71 545 28 7 13 3057 302 40 18 28 875 82 n.d n.d n.d n.d. n.d. . . . 9 13 1833 122 32 18 22 419 35 2 63 79 332 30 H1 Cycle 3 Cycle 4 pH CS R.a R.b G’3 G’’3 CS R.a R.b G’4 G’’4 (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) 5 5 80 93 506 24 5 86 100 506 20 7 n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. n.d. 9 3 48 65 217 29 4 59 n.d. n.d. 20 D) Salt stability and regeneration behavior of peptide-dextran hybrids (40kg/mol or 150kg/mol dextran backbone with peptide grafts, 1wt% hydrogels) Table 12: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.a and R.b describe G’ regeneration after 13s or 1000s after the liquefying strain was removed, respectively. G’1 - G’2 give G’ after a regeneration time of 1000s in cycle 1-2, respectively. “+ NaCl” indicates addition of 5wt% NaCl. Preparation of gels and rheology method for these experiments are indicated in chapter 2.2xv. M8: 1.3ai, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. M9: 1.3aii, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. Compound Initial Cycle 1 Cycle 2 FR G’i G’’i CS R.a R.b G’1 G’’1 CS R.a R.b G’2 G’’2 (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1^M8 13 2605 279 7 46 64 1671 166 6 53 85 1419 139 H1^M8 13 1550 100 3 32 90 1395 74 3 48 80 1121 51 +NaCl H9^M9 19 5044 456 10 27 29 1443 134 2 75 70 1006 94 H9^M9 19 2864 189 31 32 51 1456 109 2 64 102 1483 112 +NaCl E) Temperature stability of peptide-dextran hybrids with analysis of regeneration behavior Samples were prepared according to 1.3ai and rheology measurements were conducted according to method 2.2ix using setup 2.2a. Mechanical properties of H1 in regard to temperature (40 kg/mol dextran backbone with peptide grafts, 1wt% hydrogels) i) Heating from 20°C to 60°C Table 13: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’ and G’’ are listed in regard to the temperature. The sample was heated from 20°C to 60°C in steps of 5°C. Preparation of gels and rheology method for these experiments are indicated in chapter 2.2ix and 2.2xiii. M10: 1.3ai, 2.2a (parallel plate), 2.2ix, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 20°C, oscillatory time sweep 0.05% strain, 1 Hz, 20°C. Compound 20°C 25°C 30°C 35° FR G’ G’’ G’ G’’ G’ G’’ G’ G’’ (%) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) H1^M10 13 2699 222 2535 208 2326 270 2096 296 Compound 40°C 45°C 50°C 55° FR G’ G’’ G’ G’’ G’ G’’ G’ G’’ (%) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) H1 ^M10 13 1859 299 1657 306 1510 277 1449 243 Compound 60°C FR G’ G’’ (%) (Pa) (Pa) H1 ^M10 13 1278 281 ii) Cooling from 60°C to 20°C Table 14: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’ and G’’ are listed in regard to the temperature. The sample was cooled from 60°C to 20°C in steps of 5°C. V = Deviation of tan δ at a certain temperature when compared to the heating measurement. Preparation of gels and rheology method for these experiments are indicated in chapter 2.2ix and 2.2xiii. M10: 1.3ai, 2.2a (parallel plate), 2.2ix, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 20°C, oscillatory time sweep 0.05% strain, 1 Hz, 20°C. Compound 60°C 55°C 50°C FR G’ G’’ V G’ G’’ V G’ G’’ V (%) (Pa) (Pa) (%) (Pa) (Pa) (%) (Pa) (Pa) (%) H1^M10 13 1241 282 +3 1312 297 +26 1440 218 -17 Compound 45°C 40°C 35°C FR G’ G’’ V G’ G’’ V G’ G’’ V (%) (Pa) (Pa) (%) (Pa) (Pa) (%) (Pa) (Pa) (%) H1^M10 13 1538 252 -11 1677 174 -35 1700 213 -11 Compound 30°C 25°C 20°C FR G’ G’’ V G’ G’’ V G’ G’’ V (%) (Pa) (Pa) (%) (Pa) (Pa) (%) (Pa) (Pa) (%) H1^M10 13 1805 204 -3 1945 175 +9 2081 146 -15 iii) Regeneration behavior after heating to 60°C and cooling back to 20°C: G’ and G’’ are listed in regard to the temperature at 0.1% strain Table 15: Functionalization rates (FR) were determined via 1H NMR and describe the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.a and R.b describe G’ regeneration after 13s or 1000s after the liquefying strain was removed, respectively. G’1 - G’2 give G’ after a regeneration time of 1000s in cycle 1-2, respectively. Preparation of gels and rheology method for these experiments are indicated in chapter 2.2ix and 2.2xiii. M10: 1.3ai, 2.2a (parallel plate), 2.2ix, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 20°C, oscillatory time sweep 0.05% strain, 1 Hz, 20°C. Initial Cycle 1 Cycle 2 FR G’_i G’’_i CS R._a R._b G’₁ G’’₁ CS R._a R._b G’₂ G’’₂ (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) (%) (%) (%) (Pa) (Pa) H1^M10 13 2117 174 4 27 33 705 36 4 67 71 500 30 Regeneration behavior of peptide-dextran hybrid was retained even after a heating (60°C) and cooling (20°C) cycle. 4.2.2 Composite materials A) Adjustability of mechanical properties (analysis of G’, G’’, and regeneration behavior) via preparation of different composite materials by adding the unmodified polysaccharide backbone (i.e, dextran) or free peptides. Base material is H1. Table 16: P4-M: 0.5wt% H1 with 0.5wt% of P4 monomer, preparation method 2.4bi (P4 peptide which was used directly as monomer). P1-F: 0.5wt% H1 with 0.5wt% of P1 fibrils, preparation method 2.4bii (P1 peptide which was self-assembled into fibrils from P4 after pH-switch). P5: 0.5wt% H1 with 0.5wt% of P5 monomer, preparation method 2.4bi (P5 peptide which was used directly as monomer). Dextran-40: 0.5wt% H1 with 0.5wt% of dextran MW 40 kg/mol, preparation method 1.3bii(3). For H1 the functionalization rate (FR) is 13%, determined via 1H NMR, and describes the percentage quantity of dextran glucose units that are functionalized with peptide grafts. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.b describes G’ regeneration after 1000s after the liquefying strain was removed. G’1 - G’2 give G’ after a regeneration time of 1000s in cycle 1-2, respectively. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M11: 2.4bi, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. M12: 2.4bii, 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. M13: 1.3bii(3), 2.2a (parallel plate), 2.2iv, oscillatory strain sweep 0.01 - 1000% strain, 1 Hz, 25°C, oscillatory time sweep 0.1% strain, 1 Hz, 25°C. Composite Initial Cycle 1 Cycle 2 compound, portion wt% G’_i G’’_i CS R._b G’₁ G’’₁ CS R._b G’₂ G’’₂ (%) (Pa) (Pa) (%) (%) (Pa) (Pa) (%) (%) (Pa) (Pa) P4-M^M11 0.5 5779 639 6 26 1512 171 2 101 1532 165 P1-F^M12 0.5 4304 342 3 33 1407 129 2 74 1038 106 P5^M11 0.5 2936 231 2 66 1929 195 1 76 1467 154 Dextran- 0.5 2029 166 2 46 935 72 2 82 764 58 40 ^M13 Addition of negatively charged self-assembling peptide (e.g., P5) to hybrid with positively charged self-assembling peptide grafts (e.g., H1) benefited regeneration efficiency of the hydrogel after high strain conditions. Notably, composites of the hybrid and dextran were able to retain a similar regeneration efficiency compared to the hybrid alone, while G’ is reduced. B) Composites of peptide-dextran hybrids and other polysaccharides, e.g., H5 with Xanthan gum Table 17: Peptide-dextran hybrid - X.gum composite hydrogels No.5-7 according to 1.3bi Table 3. G’i gives the G’ before liquefying strain was applied at 0.1% strain. R.b describes G’ regeneration after 300s after the liquefying strain was removed, respectively. CS = Crossover strain with gel to sol transition (G’ = G’’). G’1 - G’2 give G’ after a regeneration time of 300s in cycle 1-2, respectively. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M14: 1.3bi, 2.2a (parallel plate), 2v, oscillatory strain sweep 0.01 - 100% strain, 1 Hz, 20°C, oscillatory time sweep 0.1% strain, 1 Hz, 20°C. Composite Portion Initial Cycle 1 Cycle 2 H5^total wt% G’_i G’’_i CS R._b G’₁ G’’₁ CS R._b G’₂ G’’₂ (%) (Pa) (Pa) (%) (%) (Pa) (Pa) (%) (%) (Pa) (Pa) 5 0.2 38 12 64 95 36 11 64 97 35 11 6 0.8 1286 190 24 90 1159 172 15 110 1280 187 7 0.4 169 22 36 104 176 24 26 118 205 28 Table 18: Peptide-dextran hybrid - X.gum composite hydrogels No.5-7 (C) according to 1.3bi Table 3. G’i gives the G’ before liquefying strain was applied at 0.1% strain. G’1 - G’10 give G’ after a regeneration time of 300s in cycle 1-10, respectively. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M15: 1.3bi, 2.2a (parallel plate), 2.2vi, rheological recovery test: Combined measurements of consecutive oscillatory time sweeps with alternating high strain (200%, 120 s) and low strain (0.1%, 120 s) at 20 °C with a fixed frequency of 1 Hz. Up to 10 repetitions were performed. C Initial Cycle 1 Cycle 2 Cycle 3 Cycle 4 G’i G’’i G’1 G’’1 G’2 G’’2 G’3 G’’3 G’4 G’4 (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) 5 58 17 77 19 104 23 129 29 109 27 6 877 150 903 155 938 157 940 155 945 154 7 255 49 239 47 244 48 251 49 247 48 Cycle 5 Cycle 6 Cycle 7 Cycle 8 Cycle 9 G’₅ G’’₅ G’₆ G’’₆ G’₇ G’’₇ G’₈ G’’₈ G’₉ G’’₉ (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) 5 96 25 85 21 75 20 73 19 71 19 6 1003 162 976 156 981 155 1042 164 1060 166 7 261 51 255 50 260 52 245 50 259 52 Cycle 10 G’10 G’’10 (Pa) (Pa) 5 68 18 6 1066 166 7 254 52 4.2.3 Formulations Table 19: Cream - Formulation No. 1. G’ⁱ gives the G’ before liquefying strain was applied at 0.1% strain. R.b describes G’ regeneration after 300s after the liquefying strain was removed, respectively. CS = Crossover strain with gel to sol transition (G’ = G’’). G’1 - G’2 give G’ after a regeneration time of 300s in cycle 1-2, respectively. G’3 - G’12 give G’ after a regeneration time of 120s in cycle 3-12, respectively. Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 3 (formulations) and 2.2 (rheology). Cycle 1-2: M16: 3.1, 2.2a (parallel plate), 2v, oscillatory strain sweep 0.01 - 200% strain, 1 Hz, 20°C, oscillatory time sweep 0.1% strain, 1 Hz, 20°C. Cycle 3-12: M17: 3.1, 2.2a (parallel plate), 2.2vi, rheological recovery test: Combined measurements of consecutive oscillatory time sweeps with alternating high strain (200%, 120 s) and low strain (0.1%, 120 s) at 20 °C with a fixed frequency of 1 Hz. Up to 10 repetitions were performed. Initial Cycle 1 Cycle 2 G’i G’’i CS R.b G’1 G’’1 R.b G’2 G’’2 (Pa) (Pa) (%) (%) (Pa) (Pa) (%) (Pa) (Pa) 175 47 27 46 81 30 74 60 24 Cycle 3 Cycle 4 Cycle 5 Cycle 6 Cycle 7 G’₃ G’’₃ G’₄ G’’₄ G’₅ G’’₅ G’₆ G’’₆ G’₇ G’₇ (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) 72 25 65 24 62 23 59 22 60 23 Cycle 8 Cycle 9 Cycle 10 Cycle 11 Cycle 12 G’8 G’’8 G’9 G’’9 G’10 G’’10 G’11 G’’11 G’12 G’’12 (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) (Pa) 60 23 64 24 62 23 63 24 69 26 4.3 Actives Vitamin C Homogenous distribution observed throughout the clear hydrogel. Hydrogel can be inverted by glass tilting test after overnight gelation at RT. 4.4 Biodegradation The peptide-dextran hybrid H5 is “readily biodegradable” according to the biodegradation study performed according to OECD 301F. 4.5 Cytoviability Hydrogel and components were found to have excellent cytocompatibility and not have any cytotoxic effect on A549 cells within the chosen experimental setup as cell viability was observed to exceed 70% in all cases. Table 20: Cytoviability of hydrogel and components according to CellTiter-Glo® Luminescent Cell Viability Assay. The assay was performed with human lung carcinoma cell line A549 in triplets for gel preparation procedure 1.3ai and 1.3aii. Positive control: Doxorubicine. Stdev.: Standard deviation. Component/preparation 1.3ai 1.3aii viability (%) stdev. (%) viability (%) stdev. (%) blind-value 100 29 100 22 hydrogel (H5) 1% 88 15 95 18 P41% 80 7 114 13 P40.5% 97 12 n/a n/a dextran (4) 1% 81 11 156 9 dextran (4) 0.5% 111 9 n/a n/a dextran-GMA (1) 1% 123 5 158 6 dextran-GMA (1) 0.5% 112 12 n/a n/a control (buffer) 77 27 108 13 positive control 9 2 19 6 4.6 Hydrogel long-term temperature stability (macroscopic) The gel appeared good after visual inspection, even after several weeks and months. 5 Synthesis and characterization of further hybrid polymers Glycidyl methacrylate (GMA) functionalization of different polysaccharides: In a typical reaction, a polysaccharide (15 g), provided in a flask in nitrogen atmosphere, was dissolved by addition of dry dimethyl sulfoxide (DMSO, 90 mL) and stirred (approx. 30min). The mixture was heated to 40°C under stirring. 4- (Dimethylamino)pyridin (DMAP, 2.25 g) was dissolved in dry DMSO (24 mL) separately. Subsequently, GMA (4.7 or 2.3 mL, as indicated in Table 21) was added to the DMAP solution and the mixture was added to the polysaccharide solution. The reaction was stirred 20 h at 40°C. All steps were performed under nitrogen atmosphere. The reaction was purified by dialysis (molecular weight cut-off (MWCO) 3.5 kDa) in deionized water for 5 days including water exchange every 2-3 h on day one and twice a day the remaining time. The dissolved product was lyophilized. The product was obtained as white solid. Table 21: Synthesized GMA-functionalized polysaccharides (Tara Gum, Xanthan Gum and Guar Gum) GMA-functionalized Polysaccharide GMA, polysaccharide V (mL) Tara Gum-GMA 1 Tara Gum 4.7 Tara Gum-GMA 2 Tara Gum 2.3 Xanthan Gum-GMA Xanthan Gum 2.3 Guar Gum-GMA 1 Guar Gum 2.3 Guar Gum-GMA 2 Guar Gum 4.7 Synthesis of the hybrid polymers: Peptide P4 is defined in chapter 1.2. Example 5.1) The GMA-functionalized Tara Gum (Tara Gum-GMA 1, 9.7 mg) was dissolved in 0.1% trifluoracetic acid (TFA) in water (MilliQ, 0.3 mL) (A). Separately, tris- (2-carboxyethyl)-phosphin (TCEP, 3.6 mg) was dissolved in 0.1% TFA/H2O (0.32 mL) and added to the peptide (P4, 22.0 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 10,000 rpm, 22-25°C. After lyophilization for 3 days, the hybrid (Tara Gum- Hybrid 1) was obtained as white powder. Example 5.2) The GMA-functionalized Guar Gum (Guar Gum-GMA 2, 11 mg) was dissolved in 0.1% trifluoracetic acid (TFA) in water (MilliQ, 0.22 mL) (A). Separately, tris-(2-carboxyethyl)-phosphin (TCEP, 2.64 mg) was dissolved in 0.1% TFA/H2O (0.32 mL) and added to the peptide (P4, 22.0 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 10,000 rpm, 22-25°C. After lyophilization for 4 days, the hybrid (Guar Gum- Hybrid 2) was obtained as white powder. Example 5.3) The GMA-functionalized Guar Gum (Guar Gum-GMA 1, 7.4 mg) was dissolved in 0.1% trifluoracetic acid (TFA) in water (MilliQ, 0.148 mL) (A). Separately, tris-(2-carboxyethyl)-phosphin (TCEP, 1.77 mg) was dissolved in 0.1% TFA/H2O (0.248 mL) and added to the peptide (P4, 14.8 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 10,000 rpm, 22-25°C. After lyophilization for 4 days, the hybrid (Guar Gum- Hybrid 1) was obtained as white powder. Example 5.4) The GMA-functionalized Xanthan Gum (Xanthan Gum-GMA, 5 mg) was dissolved in 0.1% trifluoracetic acid (TFA) in water (MilliQ, 0.1 mL) (A). Separately, tris- (2-carboxyethyl)-phosphin (TCEP, 1.2 mg) was dissolved in 0.1% TFA/H2O (0.2 mL) and added to the peptide (P4, 10.0 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H2O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 10,000 rpm, 22-25°C. After lyophilization for 4 days, the hybrid (Xanthan Gum- Hybrid) was obtained as white powder Example 5.5) The GMA-functionalized Tara Gum (Tara Gum-GMA 2, 10 mg) was dissolved in 0.1% trifluoracetic acid (TFA) in water (MilliQ, 0.2 mL) (A). Separately, tris- (2-carboxyethyl)-phosphin (TCEP, 2.4 mg) was dissolved in 0.1% TFA/H2O (0.3 mL) and added to the peptide (P4, 20.0 mg), the mixture (B) was incubated in a shaker for 30 min at room temperature. Solution B was then added to solution A and stirred overnight (18h) at 66°C in nitrogen atmosphere (shaker 1000rpm). The reaction was purified by ultrafiltration in 0.1% TFA/H₂O using Vivaspin tubes (5x, MWCO 5kDa, PES) at 10,000 rpm, 22-25°C. After lyophilization for 4 days, the hybrid (Tara Gum- Hybrid 2) was obtained as white powder Hydrogel preparation: The hydrogel was obtained by pre-dissolving the hybrid in acidic solution and adjusting pH to approximately pH 7. For example, to obtain a 1wt% hydrogel, 0.3 mg hybrid was dissolved in 15 µL 0.1%TFA/H₂O (pH 2). Subsequently, gelation was initiated upon addition of 15 µL 300 mM phosphate buffer pH 9 to adjust the pH to neutral (pH 7). Characterization / Rheology: Hydrogels were directly prepared on the rheology plate (8mm, plate/plate geometry with solvent trap) and the following measurement performed: (α) Time sweep (gelation curve): Oscillatory time-sweep measurements were performed at a fixed strain and fixed frequency within the range of 0.05 – 1% strain and 1 – 1.6 Hz frequency at 20 °C. (β) Thixotropy measurement 3: Consecutive combined measurements of an oscillatory strain sweep (0.01 – 1000%) at 20°C with a fixed frequency of 1 Hz followed by an oscillatory time sweep measurement with a fixed strain of 0.1% and frequency of 1 Hz for 300 s at 20 °C were conducted to analyze the strain resistance (oscill. strain sweep) and self-healing capacity of the hydrogels. Notably, the regenerative capacity of hydrogels was qualitatively assessed with “yes” if G`> G´´ or “no” if G`< G´´ after removal of high strain. The results are shown in Table 22. Table 22: Adjustability of mechanical properties of hydrogels in dependency of hybrid backbone. In contrast to the hybrids, the plain backbones were capable of weak rheology modification. Using the hybrids at 1w%, G’ was adjustable in a broad range. n.d. = not determined. CS = Crossover strain with gel to sol transition (G’ = G’’). Preparation method and rheology measurement method are indicated for each data set with corresponding reference to chapters 1.3 (hydrogel preparation) and 2.2 (rheology). M⁰⁰¹: 1.3aii, 2.2a (8 mm parallel plate), 2.2α, G’ and G’’ at 0.1% strain, 1 Hz, 20°C. M⁰⁰²: 1.3aii, 2.2a (8 mm parallel plate), 2.2β, G’ and G’’ at 0.1% strain, 1 Hz, 20°C. GMA-functionalized G’ (Pa) G’’ (Pa) CS (%) Recovery polysaccharide or 13s hybrid polymer Tara Gum-GMA 1 75 ^M001 45 ^M001 n.d. n.d. Tara Gum-Hybrid 1 15,460 ^M002 1,191 ^M002 19.1 ^M002 Yes ^M002 Tara Gum-GMA 2 276 ^M001 78 ^M001 7.8 ^M002 Yes ^M002 Tara Gum-Hybrid 2 941 ^M002 123 ^M002 16.7 ^M002 Yes ^M002 Xanthan Gum-GMA 351 ^M002 100 ^M002 5.6 ^M002 Yes ^M002 Xanthan Gum-Hybrid 1,099 ^M002 168 ^M002 33.0 ^M002 Yes ^M002 Guar Gum-GMA 1 294 ^M002 84 ^M002 7.8 ^M002 Yes ^M002 Guar Gum-Hybrid 1 2,162 ^M002 257 ^M002 22.3 ^M002 Yes ^M002 Guar Gum-GMA 2 84 ^M001 32 ^M001 n.d. n.d. Guar Gum-Hybrid 2 1,950 ^M002 229 ^M002 20.7 ^M002 Yes ^M002 As shown in Table 22, the hybrid polymers and hydrogels of the present invention have excellent rheological properties. G’ and G’’ increase significantly, as compared to polysaccharide polymers without peptide chains. A variety of polysaccharides polymers can be used, including charged and uncharged polysaccharides polymers. Example Compositions The following Example Compositions comprise Hybrid H, which is the hybrid polymer of the present invention, in particular any of the hybrid polymers H1 to H11 (as defined in Table 2) or the hybrid polymers listed in Table 22 (Tara Gum-Hybrid 1, Tara Gum-Hybrid 2, Xanthan Gum-Hybrid 1, Guar Gum-Hybrid 1, or Guar Gum- Hybrid 2). % as used herein refers to wt.-%, based on the total weight of the composition. Example Composition 1: After Sun Cream Gel Mineral Oil 3.00 % Isopropyl Palmitate 3.00 % Cetearyl Isononanoate 3.00 % Jojoba Oil 3.00 % Walnut Oil 3.00 % Tocopheryl Acetate 1.00 % Hybrid H 1.20 % Water ad 100 % Glycerin 3.00 % Allantoin (Clariant) 0.20 % Nipaguard^® POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Panthenol 1.00 % Collagen nativ 1 % 3.00 % Ethanol 1.50 % Example Composition 2: Sun Milk SPF 15 Ethylhexyl Stearate 7.00 % Decyl Oleate 5.00 % Plantasens^® Natural Emulsifier HE 20 (Clariant) 3.00 % Cetearyl Glucoside (and) Sorbitan Olivate Dimethicone 2.00 % Octocrylene 7.00 % Butyl Methoxydibenzoylmethane 2.50 % Ethylhexyl Salicylate 4.50 % Water Ad 100 % Glycerin 3.00 % Hybrid H 1.00 % Nipaguard^® POM (Clariant) 1.00 % Phenoxyethanol (and) Piroctone Olamine (and) Methylparaben Citric Acid q.s. Example Composition 3: Liquid Soap Water Ad 100 % Glycerin 3.00 % 1,2-Propanediol 2.00 % Hybrid H 3.00 % Genapol^® LRO liquid (Clariant) 20.00 % Sodium Laureth Sulfate Genagen^® CAB 818 (Clariant) 4.00 % Cocamidopropyl Betaine GlucoTain^® Clear (Clariant) 2.00 % Capryloyl/Caproyl Methyl Glucamide Nipaguard^TM DMDMH (Clariant) 0.40 % DMDM Hydantoin Fragrance 0.20 % Sodium Cloride 0.50 % Citric Acid 0.10 % Example Composition 4: Effect Shower Gel Genapol^® LRO liquid (Clariant) 30.00 % Sodium Laureth Sulfate Genagen^® CAB 818 (Clariant) 6.00 % Cocamidopropyl Betaine Hostapon^® KCG (Clariant) 5.00 % Sodium Cocoyl Glutamate Water Ad 100 % Hybrid H 1.40 % Nipaguard^® DMDMH (Clariant) 0.50 % DMDM Hydantoin Cirebelle 104 Blue 1.00% Synthetic Wax Example Composition 5: Facial Cleanser Water Ad 100 % Hybrid H 1.80 % Genapol^® LRO paste (Clariant) 4.50 % Sodium Laureth Sulfate Medialan^® LD (Clariant) 13.50 % Sodium Lauroyl Sarcosinate Genagen^® CAB 818 (Clariant) 3.00 % Cocamidopropyl Betaine Citric Acid q.s. Benzoic Acid 0.50 % Example Composition 6: Mascara Hydroxyethylcellulose 0.50 % Hybrid H 0.50 % 1,2-Propyleneglycol 1.00 % Magnesium Aluminium Silicate 1.00 % Triethanolamine 99% 1.50 % Water Ad 100 % Stearic Acid 3.00 % SilCare^® Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone SilCare^® Silicone 31M50 (Clariant) 2.00 % Caprylyl Trimethicone Tego^® Care 450 4.00 % Polyglyceryl-3 Methylglucose Distearate Polybutene. 2.00 % Beeswax 2.50 % Plantasens^® Olive Wax S51 (Clariant) 2.50 % Hydrogenated Olive Oil Microcrystalline Wax 3.50 % Iron Oxides 10.0 % Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Baycusan^® C 1004 2.00 % Polyurethane-35 Example Composition 7: BB Cream SPF 15 Water Ad 100 % Glycerin 2.00 % Hybrid H 1.00 % Hostaphat^® KW 340 D (Clariant) 3.00 % Triceteareth-4 Phosphate Cetearyl Alcohol 2.00 % Octocrylene 7.00 % Butyl Methoxydibenzoylmethane 2.50 % Ethylhexyl Salicylate 4.50 % Plantasens^® Olive LD (Clariant) 2.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables 12-15 Alkyl Benzoate 8.00 % Plantasens^® Olive Squalane (Clariant) 2.00 % Squalane Plantasens^® Shea Butter (Clariant) 1.00 % Butyrospermum Parkii (Shea) Butter XIAMETER^® PMX-200 Silicone Fluid 200 CS 2.00 % Dimethicone Chroma-Lite^® Black 0.05 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite^® Red 0.20 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite^® Yellow 0.60 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Titanium Dioxide 5.00 % Butylene Glycol 4.00 % Plantasens^® Natural Vitamin E (Clariant) 1.00 % Tocopherol Panthenol 0.50 % Gatuline^® Age Defense 2 1.00 % Aqua (and) Juglans Regia (Walnut) Seed Extract Sodium Hyaluronate 0.40 % Orgasol^® 4000 EXD NAT COS Caresse 1.00 % Nylon-6/12 Fragrance 0.20 % Nipaguard^® POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Citric Acid q.s. Example Composition 8: O/W Foundation Water Ad 100 % Hybrid H 1.00 % Magnesium Aluminium Silicate 1.00 % Plantasens^® Natural Emulsifier HP10 (Clariant) 4.50 % Sucrose Polystearate, Cetearyl Alcohol, Olea Europaea (Olive) Oil Unsaponifiables SilCare^® Silicone 31M50 (Clariant) 2.00 % Caprylyl Trimethicone XIAMETER^® PMX-200 Silicone Fluid 100 CS 2.00 % Dimethicone Caprylic/ Capric Triglyceride 5.00 % Plantasens^® Olive Wax S51 (Clariant) 1.50 % Hydrogenated Vegetable Oil Chroma-Lite^® Black 0.10 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite^® Red 0.40 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Chroma-Lite^® Yellow 1.20 % Mica (and) Bismuth Oxychloride (and) Iron Oxides Titanium Dioxide 7.00 % Dicaprylyl Carbonate 4.00 % Butylene Glycol 3.00 % Plantasens^® Natural Vitamin E (Clariant) 1.00 % Tocopherol Orgasol^® 4000 EXD NAT COS Caresse 1.00 % Nylon-6/12 Fragrance 0.20 % Nipaguard^® POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Citric Acid q.s. Example Composition 9: Liquid Highlighter Water Ad 100 % Bentonite 1.00 % Hybrid H 1.00 % Liquiwax™ PolyIPL 2.00 % Stearyl/PPG-3 Myristyl Ether Dimer Dilinoleate Plantasens^® Olive Wax S51 (Clariant) 2.00 % Hydrogenated Olive Oil Stearic Acid 1.20 % Isostearic Acid 0.90 % Water 5.00 % Sodium Hydroxide 0.12 % Orgasol^® 4000 EXD NAT COS Caresse 1.50 % Nylon-6/12 Timiron^® Super Gold 2.50 % Mica, Titanium Dioxide Xirona^® Indian Summer 2.50 % Silica (and) Iron Oxides Panthenol 0.50 % Cyclopentasiloxane 7.50 % Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Tocopheryl Acetate 1.00 % Example Composition 10: Lipstain Water Ad 100 % Glycerin 30.00 % Hybrid H 3.00 % FD&C Red No.40 0.15 % CI16035 Emulsogen^® HCO 040 (Clariant) 0.50 % PEG-40 Hydrogenated Castor Oil Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Flavour 0.20 % Example Composition 11: Eyeliner Gel Water Ad 100 % Glycerin 1.00 % Hybrid H 2.00 % Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben PVP 1.50 % Water 10.00 % Timiron^® Super Gold 12.00 % Mica, CI77891, Titanium Dioxide Example Composition 12: After Shave Balm Hostaphat® KL 340 D (Clariant) 2.00 % Trilaureth-4 Phosphate Octopirox® (Clariant) 0.05 % Piroctone Olamine Plantasens® Abyssinian Oil (Clariant) 2.00 % Crambe Abyssinica Seed Oil Isopropyl Isostearate 3.00 % Plantasens® Inca Inchi Serum (Clariant) 1.00 % Plukenetia Volubilis Seed Oil (and) Phytosterols (and) Olea Europaea (Olive) Oil Unsaponifiables (and) Beeswax Water Ad 100 % Polyglykol 400 (Clariant) 3.00 % PEG-8 Allantoin 0.30 % Hybrid H 1.50 % Dimethicone 1.00 % Citric Acid q.s. Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Example Composition 13: Sprayable Body Milk Hostaphat^® KL 340 D (Clariant) 1.00 % Trilaureth-4 Phosphate Mineral Oil 8.00 % Isopropyl Palmitate 3.00 % Cetearyl Alcohol 0.50 % Caprylic/ Capric Triglyceride 2.00 % Glyceryl Stearate 0.50 % SilCare^® Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone Hybrid H 1.00 % Water ad 100 % Glycerin 5.00 % Ethanol 5.00 % Tocopheryl Acetate 1.00 % Nipaguard^® POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Example Composition 14: Body Lotion for Men Caprylic/Capric Triglyceride 3.50 % Plantasens^® Olive LD (Clariant) 3.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables Myristyl Myristate 2.50 % Cetearyl Alcohol 2.00 % Octyldodecanol 1.00 % Glyceryl Stearate Citrate 1.50 % Hybrid H 1.20 % Water ad 100 % Glycerin 5.00 % Ethanol 3.00 % Tocopheryl Acetate 1.00 % Aloe Barbadensis Leaf Juice 1.00 % Nipaguard^® POM (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Piroctone Olamine Fragrance 0.20 % Sodium Hydroxide q.s. Example Composition 15: Anti-Aging Cream Gel Caprylic/Capric Triglyceride 5.00 % Dicaprylyl Ether 5.00 % Cetearyl Alcohol 2.00 % Nipaguard^® POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Ubiquinone 0.10 % Aristoflex^® HMB (Clariant) 0.40 % Ammonium Acryoyldimethyltaurate/ Beheneth-25 Methacrylate Crosspolymer Hybrid H 0.40 % Sodium Hyaluronate 0.30 % Water Ad 100 % Tocopheryl Acetate 0.30 % Fragrance 0.30 % Example Composition 16: Light Day Cream Water Ad 100 % Hybrid H 0.75 % Glycerin 3.00 % Plantasens^® Natural Emulsifier HE20 (Clariant) 1.20 % Cetearyl Glucoside, Sorbitan Olivate Aristoflex^® AVC (Clariant) 0.10 % Ammonium Acryloyldimethyltaurate / VP Copolymer Plantasens^® Abyssinian Oil (Clariant) 3.00 % Crambe Abyssinica Seed Oil Octyldodecanol 5.00 % Isodecyl Neopentanoate 3.00 % Plantasens^® Natural Vitamin E (Clariant) 0.50 % Tocopherol Nipaguard^® SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.30 % Citric Acid q.s. Example Composition 17: Caring Night Cream Water Ad 100 % Glycerin 2.00 % Hybrid H 1.00 % Hostaphat^® KW 340 D (Clariant) 2.00 % Triceteareth-4 Phosphate Plantasens^® Oat Serum (Clariant) 3.00 % Avena Sativa (Oat) Kernel Oil (and) Phytosterols (and) Olea Europaea (Olive) Oil Unsaponifiables (and) Beeswax Plantasens^® Shea Butter (Clariant) 7.00 % Butyrospermum Parkii (Shea) Butter Isopropyl Palmitate 5.00 % Macadamia Integrifolia Seed Oil 4.00 % Cera Alba (Beeswax) 3.00 % Nipaguard^® SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.30 % Sodium Hydroxide 0.10 % Example Composition 18: Sprayable Hair Styling Gel Hybrid H 0.90 % Water Ad 100 % Genapol^® LA-230 (Clariant) 4.00 % Laureth-23 Diaformer^® Z-632N (Clariant) 4.50 % Acrylates/Stearyl Acrylate/Ethylamine Oxide Methacrylate Copolymer Dipropylene Glycol 1.00 % Polyglykol 400 0.50 % PEG-8 Nipaguard™ DMDMH (Clariant) 0.50 % DMDM Hydantoin Panthenol 0.50 % Emulsogen^® HCO 040 (Clariant) 0.50 % PEG-40 Hydrogenated Castor Oil Fragrance 0.30 % Example Composition 19: Conditioning Shampoo Water Ad 100 % Hybrid H 1.10 % Genapol^® LRO liquid (Clariant) 30.00 % Sodium Laureth Sulfate Genagen^® CAB 818 (Clariant) 6.00 % Cocamidopropyl Betaine XIAMETER^® PMX-200 Silicone Fluid 50 CS 0.25 % Dimethicone Water 10.00 % Jaguar^® C-162 0.20 % Hydroxypropyl Guar (and) Hydroxypropyl Guar Hydroxypropyltrimonium Chloride Citric Acid q.s. Water 4.00 % Sodium Benzoate 0.45 % Sodium Chloride 0.50 % Example Composition 20: Nail Varnish Remover Gel Water Ad 100 % Ethanol 27.00 % Polyglykol^® 400 (Clariant) 3.00 % PEG-8 Glycerin 3.00 % Aristoflex^® TAC (Clariant) 0.20 % Ammonium Acryloyldimethyltaurate/ Carboxyethyl Acrylate Crosspolymer Hybrid H 1.00 % Ethyl Acetate 30.00 % Example Composition 21: Whitening Gel Genapol^® T 250 (Clariant) 2.00 % Ceteareth-25 Genapol^® DAT 100 (Clariant) 1.10 % PEG-150 Polyglyceryl-2 Tristearate Water Ad 100 % Ascorbic Acid 2- Glucoside 3.00 % Sodium Hydroxide q.s. Hybrid H 1.50 % Nipaguard^TM DMDMH (Clariant) 2.00 % DMDM Hydantoin Example Composition 22: O/W Self-Tanning Cream Hostaphat^® CC 100 (Clariant) 1.00 % Cetyl Phosphate Glyceryl Stearate 0.50 % Cetearyl Alcohol 0.50 % Mineral Oil 8.00 % Isopropyl Palmitate 7.00 % Tocopheryl Acetate 1.00 % SilCare^® Silicone 41M15 (Clariant) 1.00 % Caprylyl Methicone Hybrid H 2.00 % Water ad 100 % Hostapon^® KCG (Clariant) 0.50 % Sodium Cocoyl Glutamate Glycerin 5.00 % Fragrance 0.20 % Phenonip^TM ME (Clariant) 1.00 % Phenoxyethanol, Methylparaben, Ethylparaben Dihydroxyacetone 5.00 % Water 8.00 % Sodium Hydroxide q.s. Example Composition 23: Make Up Remover Water ad 100 % Glycerin 3.00 % Hybrid H 0.80 % Hostaphat^® KL 340 D (Clariant) 3.00 % Trilaureth-4 Phosphate Cetearyl Alcohol 1.50 % Plantasens^® Olive LD (Clariant) 2.00 % Hydrogenated Ethylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables Isostearyl Isostearate 4.00 % Isohexadecane 4.00 % Sodium Hydroxide q.s. Nipaguard^® SCP (Clariant) 1.00 % Phenoxyethanol (and) Sorbitan Caprylate Fragrance 0.20 % Example Composition 24: Insect Repellent Lotion Diethyl Toluamide 10.00 % DEET Hostaphat^® KL 340 D (Clariant) 1.00 % Trilaureth-4 Phosphate Isohexadecan 5.00 % C12-15 Alkyl Benzoate 5.00 % Cyclopentasiloxane 2.00 % Hybrid H 1.00 % Water Ad 100 % Ethanol 10.00 % Fragrance 0.30 % Nipaguard^® POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Example Composition 25: Emulsifier-free Cream Gel Caprylic/Capric Triglyceride 3.00 % Glycine Soya (Soybean) Oil 1.00 % Isopropyl Palmitate 3.60 % Glycerin 1.00 % Water Ad 100 % Hybrid H 1.50 % Fragrance 0.30 % Nipaguard^® POB (Clariant) 0.80 % Phenoxyethanol (and) Piroctone Olamine (and) Benzoic Acid Sodium hydroxide q.s. Example Composition 26: Sulfate-free Shampoo Hybrid H 0.5 % Water 20.0 % Glycerin 1.0 % Hostapon^® SG (Clariant) 23.0 % Sodium Cocoyl Glycinate Hostapon^® CGN (Clariant) 9.5 % Sodium Cocoyl Glutamate Lactic Acid q.s. Genagen^TM KB (Clariant) 15.0 % Coco-Betaine Water Ad.100% Perlogen^® SF 3000 (Clariant) 5.0 % Aqua (and) Glycol Distearate (and) Laureth-4 (and) Cocamidopropyl Betaine Velsan^® SC (Clariant) 1.0 % Sorbitan Caprylate Genamin^® PQ 43 (Clariant) 1.0 % Polyquaternium-43 Nipaguard^® CG 43 (Clariant) 0.1 % Methylchloroisothiazolinone (and) Methylisothiazolinone Fragrance q.s. Example Composition 27: Hair Conditioner Water Ad.100% Glycerin 3.0 % Disodium EDTA 0.1 % Hybrid H 0.5 % Cetyl alcohol 8.0 % Genamin^® KDMP (Clariant) 2.0 % Behentrimonium Chloride Plantasens^® Olive Squalene (Clariant) 2.0 % Squalene Genamin^® CTAC (Clariant) 4.0 % Cetrimonium Chloride Plantasens^® Olive LD (Clariant) 2.0 % Hydrogenated Ehtylhexyl Olivate (and) Hydrogenated Olive Oil Unsaponifiables Velsan^® SC (Clariant) 1.0 % Sorbitan Caprylate Phenoxetol^TM (Clariant) 0.5 % Phenoxyethanol Fragrance q.s.

Claims

Claims 1. A hybrid polymer comprising (a) a polysaccharide polymer; and (b) peptide chains.

2. The hybrid polymer according to claim 1, wherein the polysaccharide polymer is selected from dextran, dextrin, hyaluronic acid, chitosan, xanthan gum, fenugreek gum, tara gum, locust bean gum, carrageenan, guar gum, alginate, agar, agarose, starch, amylose, amylopectin, tragacanth gum, tamarind kernel gum, arabica gum, cherry gum, karaya gum, okra gum, cassia gum, chicle gum, konjac gum, ghatti gum, pectin, sclerotium gum, gellan gum, paramylon, paramylum, curdlan, cellulose, diutan gum, inulin, derivatives thereof and mixtures thereof.

3. The hybrid polymer according to claim 1 or 2, wherein at least 25%, preferably at least 30%, of the amino acids in the peptide chains are identical and preferably selected from hydrophobic amino acids, wherein the hydrophobic amino acids are preferably selected from leucine, isoleucine, phenylalanine, valine, tyrosine, and tryptophan, more preferably selected from leucine, isoleucine, phenylalanine, and valine, even more preferably selected from leucine, isoleucine, and phenylalanine, particularly preferably the hydrophobic amino acids are isoleucine.

4. The hybrid polymer according to any of claims 1 to 3, wherein at least 15%, preferably at least 20%, of the amino acids in the peptide chains are identical and preferably selected from charged amino acids, wherein the charged amino acids are preferably selected from lysine, aspartic acid, glutamic acid, arginine, and histidine, more preferably selected from lysine, aspartic acid, and glutamic acid, particularly preferably the charged amino acids are lysine.

5. The hybrid polymer according to any of claims 1 to 4, wherein at least 10%, preferably at least 20%, of the amino acids in the peptide chains are selected from amino acids having an amide group in the side chain, wherein the amino acids having an amide group in the side chain are preferably selected from asparagine, glutamine, and mixtures thereof.

6. The hybrid polymer according to any of claims 1 to 5, wherein the peptide chains contain at least one amino acid selected from serine, threonine, and mixtures thereof, preferably at least one serine.

7. The hybrid polymer according to any of claims 1 to 6, wherein the peptide chains are depsi peptide chains.

8. The hybrid polymer according to any of claims 1 to 7, wherein the peptide chains are selected from pea protein, hydrolyzed pea protein, soy bean protein, hydrolyzed soy bean protein, fava bean protein, hydrolyzed fava bean protein, chickpea protein, e.g. aquafaba, hydrolyzed chickpea protein, wheat protein, hydrolyzed wheat protein, rice protein, hydrolyzed rice protein, whey protein, hydrolyzed whey protein, baobab protein, hydrolyzed baobab protein, collagen protein, hydrolyzed collagen protein, plant collagen-like protein, hydrolyzed plant collagen-like protein, hemp seed protein, hydrolyzed hemp seed protein, jojoba protein, hydrolyzed jojoba protein, keratin protein, hydrolyzed keratin protein, lupine protein, hydrolyzed lupine protein, oat protein, hydrolyzed oat protein, quinoa protein, hydrolyzed quinoa protein, and mixtures thereof.

9. The hybrid polymer according to any of claims 1 to 8, wherein from 1 to 100%, preferably from 3 to 50%, more preferably from 5 to 40%, even more preferably from 8 to 30%, particularly preferably from 10 to 25%, of the monosaccharide units of the polysaccharide polymer are modified with the peptide chains, optionally through a linker.

10. The hybrid polymer according to any of claims 1 to 9, wherein the peptide chains are linked to the polysaccharide polymer, optionally through a linker, via the N-terminal amino acid of the peptide chains.

11. A blend comprising (a) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 40 to 65 wt-%, particularly preferably from 50 to 60 wt-%, of a hybrid polymer as defined in any of claims 1 to 10, based on the total weight of the blend; and (b) from 1 to 99 wt-%, preferably from 20 to 80 wt-%, more preferably from 30 to 70 wt-%, even more preferably from 35 to 60 wt-%, particularly preferably from 40 to 50 wt-%, of one or more polysaccharide polymers and/or one or more peptides, based on the total weight of the blend.

12. Use of a hybrid polymer as defined in any of claims 1 to 10 or a blend as defined in claim 11 as a rheology modifying agent.

13. A hydrogel comprising a hybrid polymer as defined in any of claims 1 to 10 or a blend as defined in claim 11, water, optionally a pH adjusting agent, and optionally an ionic strength adjusting agent.

14. The hydrogel according to claim 13, wherein the hydrogel further comprises an active ingredient, wherein the active ingredient is preferably selected from vitamins, moisturizing agents, anti-aging agents, anti-wrinkle agents, anti- inflammatory agents, amino acids, peptides, and mixtures thereof.

15. A formulation comprising (a) from 0.1 to 10 wt-%, preferably from 0.2 to 5 wt-%, more preferably from 0.3 to 3 wt-%, even more preferably from 0.4 to 2 wt-%, particularly preferably from 0.5 to 1 wt-%, of a hybrid polymer as defined in any of claims 1 to 10 or a blend as defined in claim 11, based on the total weight of the formulation; and (b) from 90 to 99.9 wt-%, preferably from 95 to 99.8 wt-%, more preferably from 97 to 99.7 wt-%, even more preferably from 98 to 99.6 wt-%, particularly preferably from 99 to 99.5 wt-%, of one or more further components, based on the total weight of the formulation.

16. The formulation according to claim 15, wherein the formulation is a cosmetic formulation, preferably a skin care formulation or a hair care formulation.