WO2013055051A1 - Peptide nanostructure and a production method therefor - Google Patents

Abstract

Provided is a compound of chemical formula 1. The compound of chemical formula 1 allows the formation of a self-assembled peptide nanostructure in a stable fashion via alignment between peptides, and allows nanostructures or thin films having outstanding material properties and versatility to be achieved. The peptide nanostructure according to the present invention can be used to advantage in the production of organic electronic materials, or biomaterials or the like.

Description

 【Specification】

 [Name of invention]

 Peptide nanostructures and preparation method thereof [Technical Field]

 The present invention relates to peptide nanostructures and methods for their preparation. Background Art

 Starting with organic light emitting diodes, there is a great need for development of new organic electronic materials required for the industry. In addition, existing inorganic base materials are showing difficulty in weight reduction and large-scale thinning, and above all, the necessity of alternative materials is emerging as the cost increases due to depletion of regressive resources. In particular, as touch panels have become a major player in the display industry, it is urgent to secure new materials that can be used as transparent electrodes.

It is expected that depleted tin oxide (ITO), which is currently used as a transparent electrode, will be depleted in the next few years (Kwak Jin-Sung, Nati. Co. un. 3, 645 (2012), cited in physics and high technology j _une 2012), As indium tin oxide enters an electrode in an electronic product, it is very urgent to replace it with an organic material. At present, organic materials are partially used industrially, but only a few, and most materials are expected to be replaced by organic materials or polymer materials in the future.

Materials used for storing or converting solar energy as alternative energy sources are also required to be replaced with organic materials due to resource depletion. However, in the case of organic electronic materials currently being developed, the yield and efficiency are low, and the lifespan is low. The problem is that it is short and the production cost is high. Specifically, in the case of CNTs, modification is difficult, and in the case of single-wall CNTs, it is difficult to commercialize due to the difficulty in mass production, and in the case of graphene It is emerging as a new material to replace ΠΌ, but commercialization of the transparent electrode requires excellent quality, large-area production, adhesion to the substrate, and there are many difficulties in meeting this. Therefore, many efforts have been made to make two-dimensional nanostructures using polymers or organic materials, but there are no clear achievements in the commercialization stage. One of them is nanostructure formation technology using peptides, which are biomaterials.

 US Patent No. 7, 179, 784 relates to surfactant peptide nanostructures and uses thereof, and discloses the use of nanotubes and drug delivery using the oligopeptides having a dipolar sequence. US Patent No. 7, 491, 699, relates to peptide nanostructures and methods for their preparation, which disclose spherical structures formed using peptides consisting of four amino acids including aromatic side chains and their use.

 However, the level of research on peptide nanostructures is in its infancy, and there is a need to develop various nanostructures using peptides and to develop their applications compared with the degree of understanding of formation mechanisms. [Detailed Description of the Invention]

 [Technical problem]

 The present invention has been made to solve the above problems, to provide a peptide capable of forming a nanostructure by self-assembly, a nanostructure using the same and a method of manufacturing the same.

[Measures to solve task]

 In one embodiment, the present application provides a compound of Formula 1

X ^ -Yn ^ b wherein X ¹ and X ² are each independently a D- or L-type natural or unnatural amino acid or derivative thereof having a side chain capable of pi-pi interaction, wherein X ¹ and X are ² is the same or different, Y is a D- or L-type natural or unnatural amino acid or derivative thereof having a charged or nucleophilic side chain capable of crosslinking formation, and _a and b are each the same or different from 1 to It is an integer of 10, n is an integer of 1-10.

In another aspect the disclosure relates to self-assembled nanostructures comprising one or more of the compounds of Formula 1. The self-assembled nanostructures may further include monomers for the production of conductive polymer films. In another aspect, the present application relates to a method for producing a self-assembled nanostructure using the compound of formula (1). The method includes the step of reacting a compound of Formula 1 under conditions favorable for the formation of self-assembled nanostructures.

 In another aspect, the present disclosure relates to a conductive polymer film comprising a compound of Formula 1 and a monomer.

 In another aspect, the present disclosure relates to a method for preparing a conductive polymer film using a compound of Formula 1, comprising reacting a compound of Formula 1 with a monomer. The method includes the step of reacting the compound of Formula 1 and monomer under conditions favorable for the formation of self-assembled nanostructures.

【Effects of the Invention】

 Temporal nanostructures comprising the compound of formula 1 according to the present invention are easy to prepare a variety of structures, in particular facing structure in water or various organic inorganic buffers, platform for the production of nanostructures having adjustable functionality due to the regular structure And a mold required for preparing a polymer conductive film. In addition, the nanostructure according to the present application may have a variety of conductivity depending on the type of the sequence employed, the thickness can be adjusted according to the reaction time of reaction, form a mixture with metal ions and the characteristics of the metal (catalyst, conductivity, reactivity, etc.) Can be used as an organic electronic material, as well as tunable peptide lenses for various purposes, floating scaffolds for cell culture, semi-active drug delivery vesicles, silver selective membranes, regular conductive polymers And biomaterials such as elastic protein mimetics and tyrosine-based catalysts.

[Brief Description of Drawings]

1 illustrates a peptide nanostructure formed of peptides of the YYACAYY sequence according to one embodiment of the present application. (A) is an optical micrograph (50 times magnification) photographing the morphological changes of the loaded peptide solution over time, and the bright area in the center is caused by backlight transmission. A total of 80 ^ YYACAYY solution (2mM) was added to the slide glass, and then over time It shows that a facet is formed. (B) is obliquely observed with a dropping peptide solution all optical microscope, showing a distinct boundary formed on the stomach surface by the planar peptide nanostructure. (C) is a transmission electron microscope (TEM) image of a film formed with a peptide of 2mM concentration. (D) is a photograph of a peptide film formed wide and thick across the water / air interface when 10 ml of peptide having a concentration of 2 mM in 10 cm diameter Petri dish was added. (E) is a schematic representation of the formation of a flat surface, a vertical cross-section of a tight lateral association and disulfide bond mediated by tyrosine of a peptide floating at an air / water interface, and a series of stacked thin nanosheets. It shows the formation of a flat surface through growth.

 Figure 2 shows a peptide nanostructure formed of the peptide of the YYCYY sequence according to another embodiment of the present application. (A) shows a flat surface structure formed on the upper surface by dropping 80 ^ peptide solution (2mM) onto a slide glass, leaving it in air for 30 minutes, and then observing it with an optical microscope. (B) is a TEM image of the peptide nanostructures formed in (A), and the formed film was transferred to a carbon coated grid and negatively amplified with an aqueous solution with 2% uranyl acetate. (C) is the same as (A) but is reacted in a non-oxygen environment (descator), unlike (A), no nanostructure is formed, indicating that the oxygen environment is important for the formation of a flat surface.

 Figure 3 is a photograph of a film nanostructure formed of a peptide of the YYCYY (A, B) or YYACAYY (C) sequence stained with a fluorescence reagent, the chromophoric reagent is bound to a hydrophobic chemical to fluoresce color Nile (Nile Red) (A) and stained with the Thioflavin (Tioflavin-T, Th-T) reagent ((B) and (C)), which is inserted into the nanostructure of the protein or peptide, and observed under an optical microscope.

4 is a result showing the effect of pH on the flat surface formation. (A) graphically depicts the time taken for the YYACAYY peptide (ImM) of 80 ^ at different pH values to form a flat surface of 2 ms size. Under pH 3.3, the peptide did not dissolve to form a white globule. Above pH 8, no flat surface was formed, and the equipotential point of the used peptide, namely pH It can be seen that the flat surface is formed most effectively near the pH 5, which corresponds to 5.8.

 Figure 5 shows the effect of the volume of the solution used to form the peptide nanostructure on the flat surface formation rate. Different volumes of solution were added dropwise onto the glass and the time was measured until the size of the flat surface became 2 mm. The smaller the dropping volume, the higher the flat surface formation rate, which is thought to be due to the accelerated evaporation of water at the interface where the film is formed. This indicates that the evaporation rate of water affects the film formation rate during film formation. It means that the size of the water droplets is large, it takes a long time to evaporate, it is estimated that the film formation rate is reduced. On the other hand, when the volume decreases below 20 ^, the surface formation rate becomes relatively large, and the formation rate of the flat surface is slowed down.

 FIG. 6 is a graph showing the tendency (number) of formation of films and nanofibers according to the peptide concentration and the assembly region where the nanostructures are formed, using TEM and AFM measurement results. The minimum concentration of film formation was 0.22 mM, and film formation increased with increasing concentration. Nanofibers were formed in bulk at a minimum concentration of 0.33 mM. Flat surface structures were observed at concentrations greater than 0.44 mM.

 Figure 7 shows the effect of the number of tyrosine in the peptide on the flat surface formation. For each peptide having the YCY, YYCYY, and YYYCYYY sequences, the relative rate of formation of the flat surface was measured at different concentrations (0.33, 0.55, 1.10, 1.65, and 2.20 mM of peptide (50 mM HEPES, pH 7.4)). Relative velocity was set based on YYCYY (1.1 mM) and then compared thereto. YCY did not form a film due to the lack of pi-pie interaction. (B) is

Show that YYCYY effectively forms a flat surface (single flat surface) at concentrations above l.lmM (C) shows that YYYCYYY forms a corrugated flat surface at l.lmM. This is due to the pi-pi interaction due to the additional tyrosine present. This indicates that by changing the functional group of tyrosine, it is possible to change the shape of the final material by controlling the pi-pi interaction. 8 is a chemical and structural analysis of the formed peptide film.

(A) is an AFM image showing a structure in which nanosheets are stacked in multiple layers (film formation for 20 minutes, Z range: 10 nm). (B) shows the vertical growth of the peptide film as a function of time. (C) is the result of the XRD analysis after collecting the formed film into a powder, the graph in the graph is an enlarged portion 13-56 degrees in the 2Θ range. (D) shows the Raman spectrum of the monomeric peptide (black line) and the film (blue line). (*) Represents the tyrosine peak, and the 503 cm ^"1 and 2568 cm ^{" 1} peaks represent -SS- bond and sulfhydryl group (-SH). Raman signals were magnified in the graph in the range of 460-540 cm ⁻¹ .

 9 is an AFM image of a YYACAYY film having a multilayer structure. (A) photographed the film which transitioned from the interface to mica 20 minutes after the start of film formation start, and the edge shows a step shape. This indicates that a single layer of nanosheets are continuously stacked to form a multi-layered multi-layered structure. The sharp edges and flat surfaces indicate that the molecular structure of the nanosheets is very well aligned.

(B) shows that the formed peptide film is uniform and smooth and the film is 320 nm to 365 nm thick. Over time the thickness of the film increased. In a siliconized glass, 80 ^ peptide solution (2 mM) was placed for 30 minutes to form a flat surface, and the formed film was transferred to mica for analysis.

 10 is an AFM image of a thin membrane formed by the peptide of YYACAYY. The film has a thickness of about 1.4 nm (1.1 mM, Z range: 10 nm), and the graph in the image is the result of cross-sectional analysis of the red line.

 FIG. 11 is a TEM image of a film formed using YYACAYY peptides at different concentrations (0.11-1. 1 mM). (A) shows the location of the sample taken at the air / water interface for TEM analysis. (B) is an image of nanostructures formed at different concentrations, taken 30 minutes after the start of film formation, showing the increase in film size with increasing concentration. The minimum amount required for film formation is about 0.22 mM. As the concentration increases, the thickness as well as the lateral expansion can be seen. It can be seen that at 1 mM the size of the film grows to cover the entire area of the grid (97 U m X 97 μιη).

12 is a TEM image of coexisting nanofibers formed using YYACAYY peptide. (A) Bulk phase for TEM analysis It is a schematic representation of the location of the sample taken from the solution. (B) is a TEM image measured for peptides of different concentrations of 0.33, 1.1, and 1.43 mM. This suggests that the formation of nanofibers is preferred in the bulk phase, and that film formation is preferred in the water-air interface, so that the type of nanostructures formed is determined by the position of the peptide. It is arranged so that the hydrophobic tyrosine residues of the peptide are located on one side due to the presence of an air phase at the interface, and the nanofibers are formed by different tyrosine positions on the bulk. Formation of nanofibers was initiated at 0.33 mM concentration and the amount of nanofibers formed increased with increasing concentration. At concentrations above 1.43 mM, twisted nanofibers formed and were wound around each other in the form of helix. Figure 13 shows the results of X-ray diffraction analysis of YYACAYY peptide. Since the film is not a single crystal and difficult to analyze at the atomic level, it was matched with the known protein structure and the calculation result by the present inventors. The large and strong peak of 13.5 A indicates the thickness of the layer, which is close to 14.0 A, the typical thickness observed in the thinnest layer by AFM analysis. 6.8 A represents the Ca-Ca 'distance, which is similar to the typical spacing found in conventional proteins with the spacing between cysteine residues of YYACAYY dimers linked by disulfide bonds (Ca-CH ₂ -SS-CH ₂ -Ca ᅳ). Do. The 4.8 A spacing is similar to the distance of the face to edge structure in the tyrosine-tyrosine bond. The 3.4 A gap corresponds to the diameter of the _α -helix strand in the backbone direction.

Figure 14 shows the mechanism of nanostructure formation of peptides with YYACAYY sequence. (A) shows the chemical structure of YYACAYY. (B) shows a hydrophobic phenol ring (red) and sulfhydryl group ( _-SH ) as a result of simulation of the conformation of a peptide having a YYACAYY sequence (500-ps molecular dynamics).

(Blue) is located opposite each other. (C) shows the structure of the YYACAYY peptide dimer observed in two different aspects. The plane formed by two Tyr2 and two Tyr6 is located at right angles to the plane of two Tyrl and two Tyr7. (D) shows the structure of the transversely associated YYACAYY peptide, showing that four neighboring dimers are associated by tyrosine-mediated pi-pie interaction, resulting in the continuous accumulation of nanosheets. The dotted lines indicate Tyrl The interaction between the hydroxy group of the phenol group and the plane of the phenol group of Tyr7 is expanded. Tyr2 and Tyr6 are shown using a ball and stick model. (E) is a detailed structure of the horizontally associated YYACAYY peptide, which is the result of analyzing the mechanical structure of two dimers (YYACAYY-YYACAYY) to understand the association mechanism between the peptides during the film formation process. The helix structure is green, tyrosine residues are red, and dimers are blue. Each monomer was represented by A, B, C and D, respectively. When the first dimer (left A, B) is packed closely with the second dimer (right C. D), Tyr7 of monomer A associates with Tyrl of monomer C through face to edge interactions. The same applies to Tyrl of monomer B and Tyr7 of monomer D. Tyr2 and Tyr6 are represented by ball and stick models. (F) is a nanosheet structure in which dimer peptides associated with pi-pi interactions are continuously stacked.

 15 shows HPLOESI mass spectrometry of YYACAYY monomers and films. (A) shows that the monomer (purity:> 97%) before forming the nanostructure shows a peak at 8.78 min and is confirmed by mass data (916.5). (B) shows the formation of a nanostructure by the peptide at the water / air interface, a new peak appeared at 10.88 min, which was found to be a dimer (1830.5) dimer, which is a disulfide bond in the peptide film Indicates.

 FIG. 16 shows the results of matrix-assisted laser desorpt ion / ionizat ion time of flight (MALDI-TOF) analysis of YYACAYY monomers and formed films. FIG. The appearance of a peak corresponding to the dimer at the water / air interface after film formation indicated that crosslinking was formed by the side chain of cysteine, and this peak disappeared when dithiotray (DTT) was added to the peptide solution. This indicates that disulfide bonds are important for the formation of peptide nanostructured films.

17 is a graph showing the time taken to form a flat surface according to the concentration of the reducing agent. After adding various amounts of β-mercaptoethanol to the YYACAYY peptide solution at a concentration of 1.1 mM, the time required to form a flat surface having a diameter of 2 mm was compared. As shown in the results, concentration-dependent, flat surfaces The time taken to form increased (the result is a collection of three independent experiments, with bars representing standard deviation).

 18 is a result showing the self-damage recovery ability of the peptide nanostructures. (A) shows a close-up camera photograph of the process of forming the peptide nanostructure, indicating that damage (17 minutes) generated by surface tension during the formation process is restored (26 minutes). (B) indicates that some of the peptide nanostructures formed at the interface between water and air recover within 10 minutes even if they are artificially damaged.

 19 shows that the film nanostructure formed of the peptide of the YYCYY sequence was transferred to another substrate, which shows that the large-area peptide nanostructure can be formed and can be easily transferred onto another substrate.

 20 shows 2D crystals formed by YYACAYY peptide and polypyri. (A) is a TEM image of a multilayer sheet on a carbon grid, and (B) is an AFM analysis result. 2D sheet was prepared by adding ammonium persulfate to pyrrole and YYACAYY peptide (1.1 mM) solution. The shape of the resulting film was analyzed in the height mode of the AFM. The cross section (red line) analysis shows that the sheet is very flat and homogeneous with a thickness of 5 nm (internal graph). (C) is an HRTEM image of the edges of the stacked and folded sheets, and the acceleration voltage of the TEM was 300 kV. (D) shows a high-lattice lattice image of a short sheet, showing a highly aligned crystal structure. Fourier transition of the image shows hexagonal patterns (inside).

[Form for implementation of invention]

The inventors of the present invention have an important role of aromatic amino acids such as tyrosine in the formation of self-assembled peptide nanostructures, and peptides of a specific sequence including the same can rapidly form various nanostructures in various environments through self-assembly. It is based on discovery. In one embodiment, the present application relates to a compound of Formula 1 of X—Yn—X ² b, a self-assembled nanostructure including the same, and a method of preparing the same.

Wherein X ¹ and X ² are each independently a natural or unnatural amino acid of D- or L- type having a side chain capable of pi-pi interaction. X ¹ and X ² are the same or different, Y is a D- or L-type natural or unnatural amino acid or derivative thereof having a charged or nucleophilic side chain capable of crosslinking, and a and b are each the same Or an integer of 1 to 10, and n is an integer of 1 to 10. In one embodiment according to the present application, n is 1, and a and b are each an integer of 2 to 5, and may be the same or different. In another embodiment according to the present application the a and b are the same integer between 2 and 5.

 The term "amino acid" as used herein refers to 20 naturally occurring and non-natural amino acids, amino acids that are modified after translation in vivo, such as phosphoserine and phosphothreonine; And other regressing amino acids such as 2-aminoadipic acid, hydroxylysine, nor-valine, nor-leucine; It includes modifications to enhance cell permeation or stability in vivo, and includes both the enantiomers of the D- and L-forms.

 As used herein, in the natural and unnatural the former refers to compounds in the form found in cells, tissues or in vivo, the latter means that these compounds have been artificially modified for various purposes.

As used herein, the term "peptide" refers to native amino acids or their degradation products, synthetic peptides, recombinantly prepared peptides, peptide mimetics (typically synthetic peptides), and peptides and semipeptoids, such as Peptide analogs and those modified to improve cell permeation or stability in vivo. Such modifications include, but are not limited to, N-terminal modifications, C-terminal modifications, peptide bond modifications such as CH ₂ -NH, CH ₂ -S, CH ₂ -S = 0, C¾-CH ₂ , backbone modifications, side chains. Include variations. Methods for preparing peptide mimetic compounds are known in the art and may be referred to, for example, as described in Quantitative Drug Design, CA Ramsden Gd., Choplin Pergamon Press (1992).

As used herein, the term “pi-pi interaction” refers to a bond formed by the superposition of two pi orbitals with a chemical bond formed by pi electrons. Therefore, the general formula (1) of the present application includes an amino acid having a residue capable of such interaction, for example, having an aromatic side chain Amino acids such as tyrosine, tryptophan or phenylalanine and variants, derivatives or analogs thereof.

As used herein, the term "crosslinking ^{" includes} covalent bonds or coordination bonds with metals, and may induce association of molecules by binding adjacent peptide molecules. For example, amino acid side chains include disulfide bonds through the SH group, and the amino acids capable of coordination bonds by the metal include cysteine, homocysteine, penicillamine, histidine, lysine ornithine, arginine, aspartic acid, glutamic acid, and asparagine. , Or glutamine, but not limited to the above.

In the compounds of the general formula (1) herein, Y and X ² b have amino acids having the same sequence or the symmetrical sequence with each other, in which case a and b may be the same. N- ^ a-Yn- ^ bC, including both CX ^ -Yn-X ^ -N direction, wherein N- means the amino terminal of the peptide, C- means a carboxy terminal.

 Compound of Formula 1 according to the present invention can form a nanostructure through a stable bond through self-assembly between the compounds. In particular, in the tyrosine symmetric structure having a SH group in the center, the pi bond has a two-dimensional structure, and may provide a bonding angle in which layers can be stacked (see FIGS. 13 to 17, etc.). It relates to a self-assembled nanostructure comprising a compound.

 The same or different compound of formula 1 constituting the nanostructure according to the present application can be used. In other words, a peptide having one sequence or a mixture of peptides having two or more sequences may be used to prepare a peptide nanostructure according to the present application.

^{■ In} one embodiment the peptides of Formula 1 herein are YYCYY, YYYCYYY,

YYACAYY, YYAACAAYY, YYGCGYY, YFCFY, FYCYF, FFCFF, YYAKAYY, YYAEAYY, CYY, YY, YYY, YYYY, YKCKYY, YYECEYY, YYDCDYY, YYAHAYY, YYHYY, YYAPAYY, or YYPYY or any derivative thereof. Other peptide sequences that form a nanostructure having a It is not limited to the sequence. In one embodiment of the present invention, the derivative includes an acyl derivative including those having an acetyl group at the N-terminus or a derivative having an amide group at the C-terminus.

 As used herein, the term self-assembly refers to the process by which substances such as atoms, molecules, or peptides form structures of regular shape in a particular environment. As used herein, the term “nanostructure” includes fibers, tubulars, spheres (sieves), films, the diameter or cross section of which is Ιμπι or less, in particular 500 nm, more particularly

Less than 50 nm, even more particularly less than 5 nm. In one embodiment according to the present application is 200ηηι to lnm. In the case of tubular or fiber,

Ιμπι or more, in particular 10 nm or more, more particularly lOOnra or more, even more particularly 500 nm or more.

 The peptide of the present invention may be formed in various forms depending on the conditions for forming the nanostructures. For example, peptides having a concentration of 2 mM of the same sequence can be prepared in fibers or spheres, depending on whether they are rotating or external stimuli (ultrasound) in a solvent in a two-dimensional structure at the interface. For example, the film structure is formed at the liquid-gas interface, and the nanofibers are formed in the liquid or liquid-liquid bulk phase (see FIGS. 11 and 12).

 Films formed from the peptides herein include those that comprise a facet and a planar structure. Flat surface means a film formed by overcoming the surface tension of the peptide solution as shown in Figure 1 or 2, the large surface means a film formed along the surface of the solution maintained by the surface tension.

Peptide nanostructures according to the present invention can be easily formed in large areas by self-assembly, the peptide monomer is structurally through coordination bonds, ionic bonds, hydrogen bonds, hydrophobic bonds with other peptide monomers, disulfide bonds, metal ions It grows into two-dimensional nanostructures, or planes. Cross-linkable amino acids associate peptides with other amino acids through covalent bonds, forming nanostructures with more rigid flat surfaces. By this binding, the monomer peptide forms a dimer ^' peptide, and the peptide is continuously formed by the binding of an amino acid side chain capable of pi-pi interaction in the dimeric peptide and the side-to-edge binding. Accumulation results in the formation of robust nanostructures through lateral and vertical expansion (see FIGS. 13 to 17). Therefore, in one embodiment, the nanostructures in the form of a film of the present disclosure have a single layer or a multilayer structure. In one embodiment, the thickness of the monolayer structure is about 1.4 nm, and in the case of a multilayer, various thicknesses are possible depending on the number of layers, and in one embodiment, the thickness is about 50 to 400 nm (see FIGS. 8, 9 and 10, etc.). Compounds of Formula 1 included in the assembled nanostructures may vary, and the formation rate or structure of the nanostructures may vary depending on the volume of the solution used in the preparation, the sequence of the peptide, and the concentration (FIGS. 5 and 6 And 7, etc.). In one embodiment according to the invention, the self-assembled nanostructure is a flat surface, wherein the compound of formula 1 is at least about 0.1 mM, more particularly at a concentration of about O.ltnM to lOmM, in particular at a concentration of about 0.2mM to lOmM, more particularly About 0.22 mM. In another embodiment according to the invention, the self-assembled nanostructure is a nanofiber, wherein the compound of formula 1 is at least about 0.1 mM, more particularly at a concentration of about O.lmM to 10 mM, in particular at a concentration of about 0.2 mM to 10 mM, more particularly About 0.33 mM.

 Nanostructures formed by the peptides according to the invention are formed on the liquid-gas interface or on the bulk of the liquid-liquid. The liquid forming the liquid-gas interface according to the present invention is a volatile or nonvolatile hydrophobic or hydrophilic solvent, and the gas includes, but is not limited to, air, nitrogen, helium, hydrogen, carbon monoxide, carbon dioxide, and the like. The liquid-liquid bulk phase according to the invention is formed in one embodiment at the hydrophilic and hydrophobic liquid interface, which liquid is a volatile or nonvolatile hydrophobic or hydrophilic solvent.

 Various solvents capable of forming the nanostructures according to the present application can be used, for example the volatile or nonvolatile hydrophobic or hydrophilic solvents constituting the liquid-gas or liquid-liquid bulk phaseol, for example water, Alcohols, hydrocarbons including halogens, dimethyl sulfoxide, dimethylformamide, dimethylformacetamide, N-methylpyridone, acetonitrile, tetradrafuran dioxane, or organic acids, but are not limited thereto.

The interface on which the nanostructures of the present disclosure are formed can be hydrophilic or hydrophobic. In the case of the peptide compound of the present application, it has an amphiphilic form, and the part having the lipophilic portion toward the air The hydrophilic part is towards the aqueous solution and the molecules are aligned. In one embodiment according to the present invention, the compound of formula I forms a nanostructure at a pH including a round point, about pH 3 to 8, especially near the isoelectric point (see FIG. 4). In another aspect the present disclosure also relates to a method of forming self-assembled nanostructures using a compound of Formula 1. The method comprises the step of reacting a compound of Formula 1 under conditions favorable to the formation of self-assembling nanostructures herein. In describing the present method, the above-described matters and repeated parts are omitted to avoid the complexity of the description. As described above, the self-assembled nanostructures according to the present disclosure may be formed in various structures under various conditions including interfacial conditions formed by various solvents and / or gases, concentrations of peptides and / or pH. (See FIGS. 4-12). Advantageous conditions for the formation of self-assembled nanostructures in one embodiment according to the present application are those of the compounds of formula (1) described herein at a concentration of at least 0.2 mM on a liquid-gas, or liquid-liquid bulk, for example described in the Examples herein. In an oxidizing atmosphere as described above, it is meant to react at a pH including an isoelectric point of the compound of Formula 1. PH including an isoelectric point means a pH of 土 4 centering on pi of each peptide used to form nanostructures at a pH near the round point, and in one embodiment according to the present invention, about pH 3 to 8.

 The monolayer thickness of the unit peptide nanostructures according to the present invention is about 1.4 nm in size, and over time, the monomers / dimers remaining in the solution continue to cause nanostructured reactions, resulting in thickening of the layers on the first nanostructures formed. do . This process can be confirmed by matching the theoretical peptide nanostructure thickness with that of experimental peptide nanostructures. Therefore, the thickness of the peptide nanostructures according to the reaction time may be adjusted (see FIGS. 8 to 10).

In addition, it is possible to control the type of nanostructures formed, as described above. In one embodiment according to the present disclosure, for example, the self-assembled nanostructures are films or nanofiber structures, the films are formed at the liquid-gas interface, and the nanofiber structures are formed on the bulk of the liquid or liquid-liquid. Herein, the above-mentioned mechanism at the liquid-gas and liquid-liquid interface forms a robust nanostructure comprising a flat surface. In this regard, in order to form nanostructures more quickly, inorganic substances such as metal ions including gold, silver, copper, zinc, iron, cobalt, and manganese may be added, or organic substances including various single molecules or polymers may be added. In this case, the binding between peptides is increased to promote the formation of nanostructures.

 Although not intended to be limited to this theory, the peptide nanostructure according to the present invention is stabilized, the molecular structure of the peptide monomer, the amino acid having a hydrophilic group and the amino acid having a hydrophobic group are placed in opposite positions, amino acids having a hydrophobic side chain It floats over the water, pointing towards the air. As a result, the peptide nanostructure having a two-dimensional structure is well formed at the interface between water and air. Peptides are bound to each other through pi-pi bonds and / or hydrophobic bonds, and crosslinks form a robust nanostructure. As the reaction is repeated, peptide nanostructures having a two-dimensional structure are stacked to form a multilayer structure (see FIGS. 13 to 17).

 In addition, the peptide may form a flat surface between the interface and the interface, in particular, between water and air, and may form a large-area nanostructure in centimeters.

 Furthermore, the present application may also prepare conductive polymer films using peptide self-assembled nanostructures formed by the compounds of the present disclosure (see FIG. 20). The conductive polymer film according to the present invention is prepared by mixing with various monomer materials, for example, through a polymerization process such as oxidation, and has a very well aligned crystal structure.

 In this respect, the present application also relates to a method for preparing a conductive polymer film using the compound and the monomer of Formula 1 according to the present application, and a conductive polymer film produced thereby.

In addition, the nanostructure formed using the compound of Formula 1 according to the present application can be complexed with gold, silver, copper, zinc, iron, cobalt, manganese and the like, and can be aligned together in a two-dimensional structure. like this Peptide nanostructures to which the metal is added may be conductors, semiconductors, or insulators depending on the type of metal.

 In one embodiment according to the present invention, when the peptide nanostructures according to the present invention contains tyrosine, it may help to transfer electrons well to other individuals. Through this, the peptide nanostructure according to the present invention can be used as an electron transfer layer or nanostructure that helps to transfer electrons well, and therefore, expensive metal inorganic materials having special electrical properties must be used. Compared to the case. There is a big advantage in cost. This conceptually indicates that even if a small amount of metal inorganic material is applied on the nanostructures according to the present invention, it is possible to have excellent electrical properties.

 Moreover, in the case of the planar surface between the interfaces shown in the peptide nanostructure according to the present application, since it is known to be involved in the intercellular fusion reaction in recent years, its importance in biological applications will be very large.

 In addition, the peptide nanostructure according to the present invention has the advantage that it can be conveniently prepared at a relatively low production cost. For example, unlike indium tin oxide (IT0), carbon nanolevers (CNT), and graphene production, it can be manufactured in water or various organic / inorganic buffers without special equipment / equipment. In addition, the addition of metal ions is expected to quickly form a robust nanostructure, which can be used in a variety of applications in many materials that require metal deposition. Hereinafter, preferred examples are provided to aid in understanding the present invention. However, the following examples are merely provided to more easily understand the present invention, and the contents of the present invention are not limited by the following examples. EXAMPLE

 Experimental Materials and Methods

 compound

 2-chlorotrityl chloride (CTC) (100-200 mesh, 1.26 mmol / g) resin-(1Η-benzotriazol-1-yl) -1,1,3,3-tetramethyluronium

Nucleus fluorophosphate (HBTU), hydroxybenzotriazole (HOBt) and Fmoc- Protected amino acids were purchased from BeadTech (Seoul, Korea), Ν, Ν- diisopropylethylamine (DIPEA), triisopropylsilane (TIPS), 3,6-dioxa-1,8-octanedithiol ( D0DT), 4- (3,6—dimethyl-1,3-benzothiazole—3-ium-2-yl) -Ν, Ν-dimethylaniline chloride (thioflavinti), β-mercaptoethanol, HEPES buffer , Uranyl acetate, and anisole were purchased from Aldrich (USA). Dichloromethane (DCM), Ν, Ν-dimethylformamide (DMF), methanol, piperidine, diethyl ether and trifluoroacetic acid (TFA), sodium hydroxide (NaOH) and hydrochloric acid (HC1) (South Korea), hydrogen peroxide (¾0 ₂ , 30 «was purchased from Junsei (Japan) Atomic force microscope (AFM) analysis

 Peptide aqueous solution drop (ImM) was placed on a glass surface treated with silicon and left at room temperature for 30 minutes to form a peptide two-dimensional structure at the interface, and the peptide two-dimensional structure was transferred to a clean silicon wafer or mica surface to obtain a surface. To remove the salts from the solvent, the peptide nanostructures adsorbed on the silicon wafer or mica surface were washed with distilled water and dried for 10 minutes. Peptide nanostructures were scanned at a rate of 0.5 Hz using an atomic force electron microscope (Dimension 3100, Veeco Instruments, Woodbury, NY) using a can traver tip with a spring constant of 21-78 N / m. Observed. Transmission electron microscope (TEM) analysis

Peptide nanostructure 20 ^ was dropped on a copper grid coated with 200 mesh carbon and dried for 5 minutes. All remaining solvent was removed using filter paper, and the peptide nanostructures were stained with 2% uranyl acetate staining reagent (Electron Microscopy Sciences). The grid was then placed in the desiccator to remove moisture. Peptide nanostructures were identified using an 80 kV transmission electron microscope (JE0L, JEM-1010). Fluorescence imaging Peptide nanostructures were stained with thioflavinti and confirmed by optical microscopy. 2 mM peptide was dissolved in 20 mM hippie buffer solvent (pH 7.4) at 90 ° C for 30 minutes and 250 μΜ thioflavinti was added. The peptide nanostructure was dropped on the glass surface to form a two-dimensional structure at the interface, the peptide nanostructure was transferred to a clean glass surface, and placed in a desiccator for 2 hours to remove water. Fluorescent stained peptide nanostructures were identified by excitation at 430 土 10 nm on a fluorescence microscope (Deltavision RT (Appl ied Precision, USA) microscope, Olympus 1X70 camera). Computer modeling research

 Computer prediction simulations of all peptide nanostructures were predicted through the Discovery Studio program (Version 3.1, Accelrys Inc., San Diego, CA). Each environment was measured by molecular behavior predictors in a Discovery Studio program called Chemistry at Harvard Macromolecular Mechanics (CHARMm). Peptide molecular structure was heated and stabilized by 0.001 ps for 10 ps at 5 ~ 1,000 degrees K. MALDI-TOF Mass Spectrometry

 2, 5-dihydroxybenzoic acid 10 mg All ions were removed and 1 ml of a solvent mixed with acetonitrile containing 0.1% trifluoroacetic acid in a 3: 7 ratio. Peptide solution (ImM, 0.5) was dried on Malditops plate and dried and treated for 5 minutes with 20 mM dithiothreitol (DTT) (20 mM, 0.5 ^) and ammonia water (8 mM, 0.5 μί). Results were obtained using an Autoflex MALDI-TOF mass spectrometer (Bruker Daltonics), Smart beam laser, and FlexControl software (Bruker Daltonics) .ESKElectrospray ionization mass spectrometry

Peptide two-dimensional structure is dissolved in methanol containing 0.5% acetic acid and high performance liquid chromatography equipment Electrospray ionization mass spectrometry (Thermo-Finnigan LCQ deca XP MS ESI— MS), Phenomenex C4 reverse-phase column (4 m, 100 3 隱) for 10 minutes at 10-65¾ The molecular weight was measured after separation.

X-ray Diffraction (XRD) Analysis

Peptide nanostructures (ImM, 1 ml) were formed at the air / water interface on the glass surface and then transferred to a silicon wafer and dried for 24 hours. Subsequently, to determine the chemical bond state and the pi bond of the peptide nanostructure, an infrared measuring instrument (Thermo Nicolet 6700 FT-I spectrometer, attenuated total reflection (ATR) accessory) was used to measure 300 cm ^-1 to 4,000 cm ^-1 (resolution, 1.93 cm ^_1 ) was measured by eight repeated scans.

Fourier transform infrared spectroscopy

Peptide nanostructures (ImM, 1 ml) were formed at the air / solution interface on the glass surface and then transferred to silicon wafers and dried for 24 hours. Subsequently, in order to check the chemical bond state and the pi-pi bond of the peptide nanostructures, an infrared measuring instrument (Thermo Nicolet 6700 FT-IR spectrometer, attenuated total reflection (ATR) accessory) was used to measure 300 cm ^"1 to 4,000 cm ^-1 ( resolution, 1.93 cm- ¹ ), was measured by 8 repetitive scans.

Peptide nanostructures (ImM, 1ml) were formed at the air / water interface on the glass surface and then transferred to a gold-coated silicon wafer and dried for 24 hours. The measurement range of 200 cm ^"1 to 3000 cm ^-1 was measured for 300 seconds on an Ipu Raman analyzer (Horiba Job i n-Yvon / LabRam Aram is Raman spectrometer (diode laser 785nm, power = lmW)). synthesis

Peptides were synthesized with 2-chlorotrityl chloride (CTC) resin (1.26 mmol / g) using the Fmoc / tBu method. After mounting the first amino acid (0.3-0.5 mraol / g), each coupling step is performed by reacting 2 equivalents of Fmoc-amino acid, 2 equivalents of HBTU, 2 equivalents of HOBt and 4 equivalents of DIPEA for 2 hours until the Kaiser test is negative It was. Solvent was used in a 1: 1 ratio of DCM and DMF. Fmoc groups were removed by reaction for 20 minutes in 20% piperidine / DMF, and the synthesized final peptide was cleaved in CTC resin by reacting for 90 minutes in 93% TFA, 2% TIPS, 2% D0DT and 3% anisole. The chopped mixture was then filtered, washed with DCM and methanol and the filtrate was concentrated in vacuo. The obtained residue was precipitated with cold (<10 ^° C) diethyl ether, centrifuged and vacuum dried. Peptides were purified by reverse phase HPLC if necessary and confirmed by MALDI T0F and ESI mass spectrometry. The purity of all synthesized peptides was at least 95%.

1-1 Tyr-Tyr-Cys-Tyr-Tyr (YYCYY) Synthesis

 Basically, peptide synthesis was performed as described above. 2 g of 2-CTC resin (substitution rate: 1.41 mmol / g), 459.54 mg of tyrosine derivative Fmoc-Tyr (tBu) -0H (1 画 οθ and 60ml of DMF were mixed well, and DIEA 331 μί (2 隱 ol) was added. After the resin was filtered, the resin was washed three times with DMF and MC, and then the resin was washed three times with DMF, MC, and methanol sequentially. It was confirmed that amino acids were introduced.

 50 ml of 20% piperidine / DMF solution was added to the choja containing 2 g of the resin obtained above, followed by reaction for 30 minutes. After washing three times with DMF, MC, and methanol, it was confirmed that the Fmoc was dropped as a positive result of the Kaiser test. 2 g of the obtained resin was added 919.08 mg (2 μl) of Fmoc-Tyr (tBu) -0H, 270.2 mg (2 μl) of HOBt, and 758.5 mg (2 μl) of HBTU, and 60 ml of DMF was added thereto. DIEA 662 μί (4 μl) was added thereto and stirred for 2 hours. After reaction, the resin was washed three times with DMF, MC, and methanol, and then the reaction result was confirmed by the Kaiser test. The resin was then treated with 20% piperidine / DMF for 30 minutes to remove Fmoc.

Fmoc-Cys (Trt) -0H 1171.4 mg (2 ′ ol), HOBt 270.2 mg (2 ′ ol), HBTU 758.5 mg (2 ′ ol), and DIEA 662 μί (4 mmol) in the same manner as above. Used to bind and wash cysteine. The resin thus obtained was treated with piperidine / DMF as described above to remove and wash Fmoc ol, and in the same manner as above, Fmoc—Tyr (tBu) -0H was combined twice in sequence and then 20% piperidine / Treatment with DMF yielded Tyr (tBu) -Tyr (tBu) -Cys (Trt) -Tyr (tBu) -Tyr (tBu) -CTC resin.

 Then, Tyr-Tyr-Cys-Tyr-Tyr was recovered from the polymer support as follows. Trifluoroacetate to resin ： Anisole ： (triisopropylsilane ： Octanedithiol (3,6-dioxa-l, 8-octanedithiol) (93 ： 3 ： 2 ： 2 ： 2) 70 ml of solution was added and reaction was carried out for 1 hour to remove all the protecting groups of the side chain, and the peptide was separated from the resin, and the resin was collected, the filtrate was collected, the resin was washed with MC and methanol, and the filtrate was collected. Concentrated and added cold diethyl ether to the concentrate, and left in a copper chamber to maximize the amount of precipitate, filtered, washed four times with diethyl ether using a centrifuge, and removed diethyl ether in vacuum. The dried peptide in white solid form was obtained in 85% yield.

1-2 Tyr-Tyr-Al a-Cys-Al a-Tyr-Tyr (YYACAYY) Synthesis

 To 2 g of Tyr (tBu) -Tyr (tBu) -CTC resin obtained in Example 1-1, 622.68 mg (2 mmol) of Fmoc-Ala-0H, 270.2 mg (2 mmol) of HOBt, and 758.5 mg (2 ′ ol) of HBTU It was dissolved in 60 ml of DMF after adding. DIEA 662 μ (4 μ ol) was added thereto and stirred for 2 hours. After reaction, the resin was washed three times with DMF, MC, and methanol, and then the result of the reaction was confirmed by the negative result of the Kaiser test. The resin was then treated with 20% piperidine / DMF for 30 minutes to remove Fmoc.

 In the same manner as above, using Fmoc-Cys (Trt) -0H 1171.44 mg (2 mmol), HOBt 270.2 mg (2 μl), HBTU 758.5 mg (2 μl), and DIEA 662 μί (4 μl) Cysteineol was bound and washed. The resin thus obtained was treated with 20% piperidine / DMF as described above to obtain Cys (Trt) -Ala-Ty tBu) -Tyr (tBu) -CTC resin.

Next, cysteine followed by alanine and tyrosine were combined in sequence to Tyr (tBu) -Try (tBu) -Ala-Cys (Trt) -Ala-Tyr (tBu) -Tyr (tBu) -CTC Obtained Resin. The Tyr-Tyr-Ala-Cys-Ala-Tyr-Tyr was recovered by treatment with the method of Example 1-1 to obtain the title peptide in 80% yield. Example 2 Formation of Nanostructures Under Various Conditions Using Peptides of Various Sequences

 2-1 Nanostructure Formation Using YYCYY and YYACAYY Peptides

 2-1-1 Nanostructure Formation on Slide Glass

0.5 mg, lrag, 1.5 mg, and 2 rag of the peptides of the YYCYY and YYACAYY sequences obtained in Example 1 were respectively prepared in 50 raM of phosphate buffer (Phosphated buffer, pH 7.4) or hipes buffer (HEPES buffer, _P H 7.4) (4- ( 2-hydroxyethyl) -1-piperazine ethane sulfonic acid, pH 7.4) was added thereto and dissolved at 90 ° C. The solution was added dropwise onto the glass surface in units of 10! Λ, 20 μΐ, 40 ≠ ， 60 μΐ, 80 ≠, 100 βΐ and left at 25 ° C in a humid atmosphere to form nanostructures on the water and air interface ( 1 and 2).

2-1-2 Nanostructure Formation on Petri Dish

 40 mg of each peptide of the sequence was added to 50 mM phosphate supernatant (pH

7.4) or 20 ml of Hipes buffer (pH 7.4) was dissolved at 90 ° C. The solution is then poured into Petri dishes in a humid atmosphere.

It was left at 25 ° C to form a nanostructure having a flat surface between the water and the atmosphere on the front of the Petri dish (see Figure 1D).

2-1-3 Preparation of Peptide Nanostructures with Metal Ions

0.5 mM, lmg, 1.5 mg, and 2 mg of each peptide were added 50 equivalents of phosphate buffer (pH 7.4) after adding 1 equivalent of iron chloride, zinc chloride, cobalt chloride, cobalt nitrate, cobalt hydrate, manganese hydroxide, or lithium hydroxide. ) Or 1 ml of HEPES buffer (pH 7.4) was added and dissolved at 90 ° C. Subsequently, each solution was dropped on a glass surface in units of 10 μ, 20 fd, 40 μΐ, 60 μ, 80 μί and 100 ≠ and left at 25 ° C in a humid atmosphere. It formed more than twice as fast. The results indicate that addition of metal ions such as zinc, iron, and cobalt may promote the formation of nanostructures due to interactions with these peptides (results not shown).

2-2 Formation of Nanostructures Using Various Peptides and Derivatives Peptides of various sequences shown in Table 1 were synthesized in the same manner as in Example 1, and each of these peptides was dissolved in 50 mM HEPES (pH 7.4) at a final concentration of l.lmM. It was. Subsequently, the nanostructure formation process was investigated for each 80-year-old solution as in Example 2-1. The results are shown in Table 1. As shown in Table 1 below, when one or more tyrosine and one or more nucleophiles, cysteine, were combined, it was confirmed that solid nanostructures having large and flat surfaces were well formed. In addition, when a tyrosine derivative (dopa having one more hydroxyl group in the meta position of tyrosine) was used, it was confirmed that nanostructures were formed on the surface.

 TABLE 1

 [O ： Tyrosine, C: Cysteine, F: Phenylalanine, A: Alanine, Ε: Glutamic acid, Κ: Lysine, S: Serine, DOPA (L-3 '4' -di hydr oxypheny 1 a 1 an i ne) ： Tyrosine Derivatives (dopa), Fmoc: Fluorenylmethyloxycarbonyl chloride] Flat surface formation in Table 1 measured the time to reach 2 mm in diameter at room temperature, very fast: formed in 1 minute , Fast: 1 minute to 30 minutes, Slow: 30 minutes to 60 minutes, Very slow: 60 minutes or more. Example 3 Characterization of the Formed Peptide Nanostructures

 3-1 Analysis of Nanostructure Surface Using Atomic Force Microscopy (AFM)

Peptides YYACAYY and YYCYY obtained in Example 1 were each dissolved at a concentration of 2 mM in 50 mM HEPES H 7.2 buffer. This solution was completely dissolved through sonication (20 minutes) and heat treatment (80 ^° C., 20 minutes). Peptide nanostructure formation was induced on the interface by dropping the solution on a glass surface and leaving it at 25 ^° C in a humid atmosphere. The surface treated mica (mica) was transferred to the peptide nanostructures and transferred to air for 5 minutes. Prepared samples were analyzed by AFM (see FIGS. 8-10). Through the AFM analysis, the self-assembly of nanostructures can be observed in detail, and the self-assembly shape, the relationship between monolayers, and the thickness or height of one monolayer can be known.

 FIG. 8A illustrates the relationship between the monolayers through monolayers and shapes generated by partially removing a portion of the layered peptide nanostructures by using a salophane tape, and FIG. 9 is a part of the nanostructures using a salopane tape as in FIG. 8A. It shows the measurement of the thickness or height of a single nanostructure through a cross-section resulting from partial removal of.

 The results of the AFM analysis confirmed that the peptide nanostructure has a typical supramolecular structure due to self-assembly. Specifically, it was confirmed that a thin layer having a thickness of about 1.4 nm corresponding to the height of the YYCYY molecular monomer was repeatedly formed on the interface with the layers stacked repeatedly (see FIGS. 8 to 10). The repetitive stacking of thin layers of this ordered arrangement is expected to drive the water to overcome the strong surface tensions seen at the interface with air and to form a flat surface where the nanostructures can be seen.

3-2 Characterization of Peptide Nanostructures by Fluorescent Dyeing

 3-2-1 Ni le Red Dyeing

Peptide nanostructures were stained using Nilered, which reacts specifically to hydrophobic environments. 2 mg / ml (2.2mM) YYCYY, 0.2 mg / ml Nilered was prepared by dissolving in a 50 mM hippie complete solution pH 7.2 containing 5% DMS0. Peptide nanostructure formation on the air / water interface was induced by dropping the solution on a 100 χ glass surface in a drop form and standing at 25 ^° C. in a humid atmosphere. The formed peptide nanostructures were transferred to a clear glass surface, and observed with a fluorescence microscope (see FIG. 3A).

The fluorescence developing reagent used for fluorescence microscopy combined with hydrophobic groups was used as a fluorescing nile fluorescence developing reagent. As shown in FIG. 3A, it was confirmed that the formed nanostructure was a peptide containing one or more tyrosine having hydrophobic properties. 3-2-2 Thioflavin-T (ThT) Staining

 In general, fluorescence analysis was performed by using thiofullevin (Thioflavin T, ThT), which is inserted between peptide nanostructures. 1 mg / ml YYCYY dissolved in 50 mM hippie buffer pH 7.2 was reacted with 50 μΜ ThT. Peptide nanostructure formation was induced on the interface by dropping the solution 100 ^ onto the glass surface in a drop form and standing at 25 ° C. in a humid atmosphere. The formed peptide nanostructures were transferred to a clear glass surface, and then observed with a fluorescence microscope (see FIG. 3).

 As shown in Figure 3B and (:, it was confirmed that the peptide containing one or more tyrosine nanostructures formed. Example 4 Analysis of the complementary properties of the defects of the formed peptide nanostructures in the peptide nanostructures formed in Example 2 Defects were made on the surface using a pair of tweezers, and self-complementary properties were analyzed by intermolecular self-assembly.The prepared peptide nanostructures actively react to damage caused by external stimuli and have the ability to heal the defects immediately. (Refer to Figure 18B) This means that the self-healing system allows self-healing immediately upon some damage to the nanostructures.

Therefore, this would be suitable for anti-scratch nanostructures, and it is also indicated that the application of a specific molecule having a very important function to the nanostructures according to the present invention is well suited for storage and delivery of specific drugs. . Example 5 Transition of Peptide Nanostructures Formed onto Secondary Substrates A high degree of utility of the peptide nanostructures formed on the interfacial interface requires transfer techniques over various substrates. In addition to the method of dipping the peptide nanostructure obtained in Example 2 onto the surface of the peptide nanostructure, the second substrate was previously placed inside the peptide solution for more stable nanostructure transfer. air As the total volume of the solution is reduced by exposure to the phase, the nanostructure naturally

Techniques for transitioning over the secondary substrate were obtained (see FIGS. 1 and 19).

 This is a new dip coating method that can replace the traditional gravure coating, mayer bar coating or spin coating. In other words, it means that the nanostructure can be applied to the substrate without specific equipment. In this way, the use of expensive coating equipment and complex coating processes can be solved. Example 6 Conductive Polymer Films Prepared by YACAYY Peptide and Polypyrrole

 Nanostructures as in Example 2 using blood (or aniline, thiophene or 3,4-ethylenedioxythiophene) and YYACAYY peptide (2 mM) in a 1: 1 molar ratio mixed in 1 ml of 50 mM HEPES followed by 100 of these After 10 minutes, a flat surface was formed. In other words, two-dimensional nanostructures were formed at the interface between solution and air. Subsequently, blood trapped between peptide two-dimensional structures using ammonium persulfate or iron (III) chloride (2 molar equivalents of monomer) as an oxidant on a blood-flat hybrid flat surface formed at the interface between the air and the solution, aniline, thiophene Or 3, 4-ethylenedioxythiophene single molecule was polymerized into a two-dimensional conductive polymer. The result was a well aligned crystal structure (see FIG. 20). The AFM analysis showed that the thickness was 5 nm, and the high-magnification TEM analysis showed that the crystal had a hexagonal structure of a = 0.445 nm (Fig. 20C, D). These results indicate that due to the regular arrangement as described above, the metallicity of the polymer film may be increased. The foregoing description of the present invention is intended for illustration, and it will be understood by those skilled in the art that the present invention may be easily modified in other specific forms without changing the technical spirit or essential features of the present invention. will be. Therefore, the embodiments described above are to be understood in all respects as illustrative and not restrictive.

Claims

 [Claim]

 [Claim 11

 Compound of Formula 1

 Χ ^ -Υη-Χ

 In the above formula

X ¹ and X ² are each independently a D- or L-type natural or non-natural amino acid having a side chain capable of pi-pi interaction or a derivative thereof, wherein X ¹ and X ² are the same or different,

 VII is a D- or L-type natural or unnatural amino acid or derivative thereof having a charged or nucleophilic side chain capable of crosslinking,

 a and b are each an integer of 1 to 10, the same or different,

 n is an integer from 1 to 10.

 [Claim 2]

 The compound of formula 1 according to claim 1, wherein the crosslinking comprises covalent bonds or coordination bonds with metals.

 [Claim 3]

 According to claim 2, wherein the amino acid capable of coordination bond by the metal is cysteine, homocysteine, penicillamine, salenocysteine, histidine, lysine, ornithine, aspartic acid, glutamic acid, asparagine, glutamine, Compound.

 [Claim 4]

 The compound of formula 1 according to claim 1, wherein the pi-pi interactable amino acid is an amino acid having an aromatic side chain.

 [Claim 5]

 The compound of formula 1 according to claim 1, wherein the pi-pi interactable amino acid is phenylalanine, tryptophan or tyrosine.

 [Claim 6]

The compound of formula 1 according to claim 1, wherein the amino acid capable of forming a crosslink is an amino acid having an SH moiety.

[Claim 7]

The compound of formula 1 according to claim 1, wherein X ^L a and X ² b have amino acids having the same sequence or the symmetrical sequence with respect to Y.

 [Claim 8]

The compound of formula 1 according to claim 1, wherein n is 1 and _a and b are integers of 2 to 5, respectively.

 [Claim 9]

 The compound of formula 1 according to claim 1, wherein n is 1 and a and b are integers of 2 to 5 equal to each other.

 [Claim 10]

 According to claim 1, wherein the compound of Formula 1 is YYCYY, YYYCYYY, YYACAYY, YYAACAAYY, YYGCGYY, YFCFY, FYCYF, FFCFF, YYAKAYY, YYAEAYY, CYY, YY, YYY, YYYY, YKC YY, YYECEYY, YYHAYY , YYAPAYY, YYPYY and derivatives thereof.

 [Claim 11]

 A self-assembling nanostructure comprising the compound of any one of claims 1 to 10.

 [Claim 12]

 The self-assembled nanostructure of claim 10, wherein the self-assembled nanostructure comprises a film, a nanofiber, or a sphere.

 [Claim 13]

 13. The self-assembled nanostructure of claim 12, wherein the film is flat or large in surface.

 [Claim 14]

The self-assembling nanostructure of claim 13, wherein the flat surface or the large surface type is a multilayer structure.

[Claim 15]

 The self-assembling nanostructure of claim 11, wherein the self-assembling nanostructure is a flat surface and the compound of Formula 1 is included at a concentration of about 0.1-10 mM or more.

 [Claim 16]

 The self-assembled nanostructure of claim 15, wherein the compound of Formula 1 is included at a concentration of about 0.22 mM.

 [Claim 17]

 The self-assembled nanostructure of claim 11, wherein the self-assembled nanostructure is a nanofiber and the compound of Formula 1 is included in an amount of about 0.1 to 10 mM.

 [Claim 18]

 The self-assembled nanostructure of claim 17, wherein the compound of Formula 1 is included at a concentration of about 0.33 mM or more.

 [Claim 19]

 The self-assembled nanostructure of claim 11, wherein the self-assembled nanostructure is formed on the liquid-gas interface or on the bulk of the liquid-liquid.

 [Claim 20]

 The liquid of claim 19, wherein at the liquid-gas interface, the liquid is a volatile or nonvolatile hydrophobic or hydrophilic solvent, and the gas is air, nitrogen, helium, hydrogen, carbon monoxide, or carbon dioxide, and the liquid-liquid bulk on the The liquid is a volatile or nonvolatile hydrophobic or hydrophilic solvent.

 [Claim 21]

21. The method of claim 20, wherein the volatile or nonvolatile hydrophobic or hydrophilic solvent is water, alcohols, hydrocarbons including halogen, dimethyl sulfoxide, dimethylformamide, dimethylformacetamide, N-methylpyridone, tedra A self-assembling nanostructure, comprising hydrfuran, dioxane, acetonitrile or organic acid.

[Claim 22]

 The self-assembled nanostructure of claim 19, wherein the bulk phase is formed at a hydrophilic and hydrophobic liquid interface.

 [Claim 23]

 The self-assembling nanostructure of claim 11, wherein the self-assembling nanostructure is formed at pH 3 to 8 including an isoelectric point of a compound of Formula 1 included in the nanostructure.

 [Claim 24]

 The self-assembled nanostructure of claim 12, wherein the film structure is formed at a liquid-gas interface and the nanofiber is formed on a liquid or liquid-liquid bulk.

 [Claim 25]

 The self-assembled nanostructure of claim 11, wherein the self-assembled nanostructure further comprises a monomer.

 [Claim 26]

 The self-assembled nanostructure of claim 25, wherein the monomer is blood, aniline, thiophene, or 3,4-ethylenedioxythiophene.

 [Claim 27]

 A conductive polymer film comprising the compound of Formula 1 and a monomer.

 [Claim 28]

 A method for producing a conductive polymer film using a compound of formula (1) comprising the step of reacting the compound of formula (1) with a monomer under conditions favorable for the formation of self-assembled nanostructures.

 [Claim 29]

 A method of forming self-assembling nanostructures using a compound of formula (1) comprising the step of reacting the compound of formula (1) under favorable conditions for forming self-assembling nanostructures.

 [Claim 30]

30. The method according to claim 29, wherein the favorable conditions for the formation of the self-assembled nanostructures are at least 0.2 mM concentration in the liquid-gas interface or the bulk of the liquid-liquid compound of Formula 1, in an oxidizing atmosphere, Reacting at a pH containing the isoelectric point of the compound, self-assembled nanostructures forming method.

[Claim 31]

 31. The self-assembly of claim 30, wherein the self-assembling nanostructure is a film or nanofiber structure, the film is formed at a liquid-gas interface, and the nanofiber structure is formed on a bulk of liquid or liquid-liquid. Nanostructure Formation Method.

 [Claim 32]

 32. The method of claim 31, wherein the method further comprises adding metal ions to the compound of Formula 1.