CN114621471A - Collagen gel and preparation method and application thereof - Google Patents
Collagen gel and preparation method and application thereof Download PDFInfo
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- CN114621471A CN114621471A CN202210342920.6A CN202210342920A CN114621471A CN 114621471 A CN114621471 A CN 114621471A CN 202210342920 A CN202210342920 A CN 202210342920A CN 114621471 A CN114621471 A CN 114621471A
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J3/00—Processes of treating or compounding macromolecular substances
- C08J3/24—Crosslinking, e.g. vulcanising, of macromolecules
- C08J3/246—Intercrosslinking of at least two polymers
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J3/00—Processes of treating or compounding macromolecular substances
- C08J3/02—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques
- C08J3/09—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques in organic liquids
- C08J3/091—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques in organic liquids characterised by the chemical constitution of the organic liquid
- C08J3/095—Oxygen containing compounds
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J3/00—Processes of treating or compounding macromolecular substances
- C08J3/02—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques
- C08J3/09—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques in organic liquids
- C08J3/091—Making solutions, dispersions, lattices or gels by other methods than by solution, emulsion or suspension polymerisation techniques in organic liquids characterised by the chemical constitution of the organic liquid
- C08J3/096—Nitrogen containing compounds
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J2389/00—Characterised by the use of proteins; Derivatives thereof
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- C—CHEMISTRY; METALLURGY
- C08—ORGANIC MACROMOLECULAR COMPOUNDS; THEIR PREPARATION OR CHEMICAL WORKING-UP; COMPOSITIONS BASED THEREON
- C08J—WORKING-UP; GENERAL PROCESSES OF COMPOUNDING; AFTER-TREATMENT NOT COVERED BY SUBCLASSES C08B, C08C, C08F, C08G or C08H
- C08J2405/00—Characterised by the use of polysaccharides or of their derivatives not provided for in groups C08J2401/00 or C08J2403/00
- C08J2405/04—Alginic acid; Derivatives thereof
Abstract
The invention belongs to the technical field of biomedical materials, and relates to a collagen gel and a preparation method and application thereof. The preparation method comprises the following steps: adding the freeze-dried collagen sponge into a polar solvent system to prepare a collagen solution, adding oxidized alginate into the collagen solution to perform a crosslinking reaction, and reacting to obtain the collagen sponge; the polar solvent system is formed by blending ionic liquid and acetic acid aqueous solution. According to the invention, the ionic liquid is introduced and matched with acetic acid, so that the electrostatic interaction between the oxidized alginate and collagen molecules can be effectively shielded, the crosslinking of collagen and the oxidized alginate is regulated, and the high-performance collagen gel is prepared. The preparation method of the gel is simple and convenient, and is suitable for industrial production.
Description
Technical Field
The invention belongs to the technical field of biomedical materials, and relates to a collagen gel and a preparation method and application thereof.
Background
The information in this background section is only for enhancement of understanding of the general background of the invention and is not necessarily to be construed as an admission or any form of suggestion that this information forms the prior art that is already known to a person of ordinary skill in the art.
Collagen gels have attracted attention because of their many excellent biological properties, including low immunogenicity and the promotion of cell adhesion and proliferation. However, the pure collagen gel has the defects of non-ideal mechanical strength, excessively fast enzymolysis rate, poor thermal stability and the like, and still can not completely meet the performance requirements of biomedical materials.
Disclosure of Invention
In order to solve the defects of the prior art, the invention aims to provide the collagen gel, the preparation method and the application thereof.
In order to achieve the purpose, the technical scheme of the invention is as follows:
on one hand, the preparation method of the collagen gel comprises the steps of adding freeze-dried collagen sponge into a polar solvent system to prepare a collagen solution, adding oxidized alginate into the collagen solution to carry out a crosslinking reaction, and reacting to obtain the collagen gel; the polar solvent system is formed by blending ionic liquid and acetic acid aqueous solution.
The chemical crosslinking can improve the defects of high enzymolysis rate, poor thermal stability and the like of the collagen gel, and the improvement effect of the aldehyde crosslinking agent is more effective. However, there are various aldehyde crosslinking agents such as glutaraldehyde, EDC, genipin, and the like. The invention adopts the oxidized alginate (OSA) as a cross-linking agent, not only can reduce the damage to tissues, but also can be used as a coupling grafting agent to combine the active aldehyde group with the bioactive substances, thereby improving the specific adhesion capability of the gel material and cells. However, OSA, a typical anionic polysaccharide cross-linking agent, is very easily strongly electrostatically attracted to positively ionized collagen molecules to form milky flocculent precipitates, which directly results in incomplete cross-linking, complete destruction of gel structure, difficulty in material shaping, and the like.
The invention adopts ionic liquid and acetic acid to mix and prepare a polar solvent system, and can effectively shield the electrostatic interaction between two polyelectrolytes, thereby obtaining the collagen-based gel biomaterial with uniformity and excellent performance.
In another aspect, a collagen gel is obtained by the above preparation method.
In a third aspect, use of the above collagen gel in the preparation of a biosensor.
In a fourth aspect, a biosensor comprises the above collagen gel as a base material.
Experiments show that the biosensor provided by the invention can effectively identify real-time feedback of omnibearing information such as action amplitude, speed, frequency and the like when an electrochemical workstation is used for collecting resistance signals when a finger is bent.
The beneficial effects of the invention are as follows:
1. the materials adopted by the collagen gel are all human body absorbable biomaterials and have good biocompatibility. Wherein, the collagen is taken as an important component of human skin and has good compatibility with human tissues; the degradation product of the oxidized alginate is a micromolecular substance which can be discharged out of the body through the metabolism of the human body, thereby avoiding the organism tissue reaction caused by the immunological rejection of the traditional gel material in the biomedical process.
2. The preparation method of the collagen gel comprises the step of introducing the ionic liquid with stronger polarity to regulate and control the crosslinking reaction of the collagen and the oxidized alginate so as to prepare the high-performance collagen gel. The cross-linking reaction efficiency involved in the preparation process is high, the operation is simple, and the economic benefit is high.
3. The mechanical strength of the collagen gel obtained by the invention is obviously improved, and a new way is provided for diversification of a collagen gel modification method.
Drawings
The accompanying drawings, which are incorporated in and constitute a part of this specification, are included to provide a further understanding of the invention, and are incorporated in and constitute a part of this specification, illustrate exemplary embodiments of the invention and together with the description serve to explain the invention and not to limit the invention.
FIG. 1 is a graph showing the tendency of the degree of crosslinking of collagen gels prepared according to various embodiments of the present invention;
FIG. 2 is a graph showing the results of a biosensor manufactured using the collagen gel of example 1 for recognizing the bending angle of a finger in an experimental example of the present invention.
Detailed Description
It is to be understood that the following detailed description is exemplary and is intended to provide further explanation of the invention as claimed. Unless defined otherwise, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs.
It is noted that the terminology used herein is for the purpose of describing particular embodiments only and is not intended to be limiting of exemplary embodiments according to the invention. As used herein, the singular forms "a", "an" and "the" are intended to include the plural forms as well, and it should be understood that when the terms "comprises" and/or "comprising" are used in this specification, they specify the presence of stated features, steps, operations, devices, components, and/or combinations thereof, unless the context clearly indicates otherwise.
The invention provides a collagen gel and a preparation method and application thereof, aiming at the defects of poor mechanical strength, excessively fast enzymolysis rate, poor thermal stability and the like of a pure collagen gel and incapability of meeting the performance requirements of biomedical materials.
The invention provides a typical embodiment of a preparation method of collagen gel, which comprises the steps of adding freeze-dried collagen sponge into a polar solvent system to prepare a collagen solution, adding oxidized alginate into the collagen solution to carry out a crosslinking reaction, and reacting to obtain the collagen gel; the polar solvent system is formed by blending ionic liquid and acetic acid aqueous solution.
The invention adopts the oxidized alginate as the cross-linking agent, not only can reduce the damage to tissues, but also can be used as a coupling grafting agent to combine the active aldehyde group with the bioactive substances, thereby improving the specific adhesion capability of the gel material and cells.
Meanwhile, the invention adopts ionic liquid and acetic acid to mix and prepare a polar solvent system which can shield electrostatic attraction generated between oxidized alginate and collagen molecules, thereby obtaining a uniform collagen-based gel biomaterial with excellent performance.
In some embodiments of this embodiment, the polar solvent system has a pH of 1.5 to 5.0. Under the condition, the prepared collagen gel has better performance.
In some embodiments of this embodiment, the ionic liquid is one or more of 1-ethyl-3-methylimidazolium acetate, 1-ethyl-3-methylimidazolium formate, and 1-butyl-3-methylchloroimidazolium acetate. The ionic liquid can better shield the electrostatic interaction between two polyelectrolytes, thereby enhancing the crosslinking degree of collagen gel and obviously improving the mechanical property.
In some examples of this embodiment, the concentration of the acetic acid solution is 0.1 to 1.0 mol/L.
In some examples of this embodiment, the volume ratio of the ionic liquid to the acetic acid solution is 9:1 to 5: 5.
In some examples of this embodiment, the collagen solution is prepared under ice-water bath conditions.
In some embodiments of this embodiment, the concentration of the collagen solution is 5-30 mg/mL.
In some examples of this embodiment, the time for the crosslinking reaction is 12 to 48 hours.
In some examples of this embodiment, the temperature of the crosslinking reaction is 2 to 10 ℃.
In some examples of this embodiment, the oxidized alginate is obtained by oxidizing alginate with an oxidizing agent.
In one or more embodiments, the oxidizing agent is sodium periodate or potassium permanganate. The oxidant can better oxidize alginate to form a plurality of aldehyde groups, and is more favorable for crosslinking with collagen.
In one or more embodiments, the mass ratio of the oxidizing agent to the alginate is 1-2: 1.
In one or more embodiments, the pH of the system during the oxidation treatment is 2 to 5.
In one or more embodiments, the time for the oxidation treatment is 12 to 48 hours.
In another embodiment of the present invention, there is provided a collagen gel obtained by the above-mentioned preparation method.
In a third embodiment of the present invention, there is provided a use of the above collagen gel for preparing a biosensor.
In a fourth embodiment of the present invention, there is provided a biosensor comprising the above collagen gel as a base material.
Specifically, the biosensor is matched with an electrochemical workstation, and when the biosensor is fixed on a finger, a resistance signal generated when the finger is bent can be collected through the electrochemical workstation.
In order to make the technical solutions of the present invention more clearly understood by those skilled in the art, the technical solutions of the present invention will be described in detail below with reference to specific embodiments.
In the following examples, the preparation method of oxidized sodium alginate comprises: weighing a proper amount of sodium alginate, adding the sodium alginate into a three-neck flask, and adding deionized water to prepare a uniform sodium alginate solution with the concentration of 20 mg/mL. The pH value of the sodium alginate solution is adjusted to 3.0 by hydrochloric acid, and then a certain volume of sodium periodate solution with the concentration of 0.11g/mL is added (the molar ratio of the sodium alginate to the sodium periodate is 1: 1). The reaction was stirred for 24h under exclusion of light. After the reaction is finished, adding excessive absolute ethyl alcohol to obtain white precipitate, namely the oxidized sodium alginate. The method is carried out by alternately using ethanol and water to remove periodate. And (4) placing the finally obtained white precipitate in a culture dish, drying the white precipitate at a room-temperature ventilated place, and sealing and storing the white precipitate for later use.
Example 1
Dissolving a freeze-dried natural cow leather collagen sponge in a polar solvent system of 1-ethyl-3-methylimidazolium acetate/acetic acid aqueous solution (volume ratio is 9:1, concentration of the acetic acid aqueous solution is 0.5mol/L) with pH of 5.0 under the condition of ice-water bath to obtain a uniform cow leather collagen solution with collagen concentration of 30 mg/mL. And slowly adding 7.5% of oxidized sodium alginate solution (dripping off after 2 min) into the collagen solution to ensure that the mass ratio of the collagen to the oxidized alginate in the final solution system is 1: 1. And fully and uniformly stirring the crosslinking solution, defoaming, and reacting for 48 hours at 4 ℃ to obtain the collagen gel.
Example 2
Dissolving freeze-dried natural pigskin collagen sponge in a polar solvent system of 1-ethyl-3-methylimidazolium formate/acetic acid aqueous solution (volume ratio is 7:3, concentration of acetic acid aqueous solution is 0.5mol/L) with pH of 3.5 under the condition of ice-water bath to obtain a uniform bovine skin collagen solution with collagen concentration of 25 mg/mL. And slowly adding 7.5% of oxidized sodium alginate solution (dripping off after 2 min) into the collagen solution to ensure that the mass ratio of the collagen to the oxidized alginate in the final solution system is 1: 1. And fully and uniformly stirring the crosslinking solution, defoaming, and reacting for 48 hours at 4 ℃ to obtain the collagen gel.
Example 3
Dissolving freeze-dried natural pigskin collagen sponge in a polar solvent system of 1-butyl-3-methyl chloroimidazole acetate/acetic acid aqueous solution (volume ratio is 5:5, concentration of the acetic acid aqueous solution is 0.5mol/L) with pH of 1.5 under the condition of ice-water bath to obtain a uniform cow skin collagen solution with collagen concentration of 20 mg/mL. And slowly adding 7.5% of oxidized sodium alginate solution (dripping off after 2 min) into the collagen solution to ensure that the mass ratio of the collagen to the oxidized alginate in the final solution system is 1: 1. And fully and uniformly stirring the crosslinking solution, defoaming, and reacting for 48 hours at 4 ℃ to obtain the collagen gel.
And (3) testing the crosslinking degree:
0.15g of collagen gel is weighed and mixed with 2mL of borax buffer solution with the pH value of 10, 2mL of freshly prepared 0.1% (v/v) 2,4, 6-trinitrobenzenesulfonic acid (TNBS) solution is immediately added, the mixture is stirred and mixed uniformly by vortex oscillation, and then the mixture is placed in a constant temperature water bath kettle at 50 ℃ to react for 60min in a dark place. After the reaction is finished, 4mL of hydrochloric acid solution with the concentration of 6mol/L is immediately added into the solution, the solution is evenly shaken and then placed into a constant-temperature water bath kettle at 60 ℃ to continue the reaction for 90min until the solution is clear. After cooling at room temperature, the absorbance of the solution was measured at 340nm using an ultraviolet-visible spectrophotometer. All samples were run in triplicate and averaged. Since the epsilon-amino group which does not participate in the reaction in the collagen reacts with TNBS, a chromogenic substance is generated. Therefore, the crosslinking degree of the modified gel can be indirectly measured by measuring the change of the absorbance value of the system, and the calculation formula is as follows:
the absorbance of the epsilon-amino groups participating in the crosslinking reaction is equal to the absorbance of all epsilon-amino groups in the native collagen-the absorbance of epsilon-amino groups not participating in the crosslinking reaction.
And quantitatively analyzing the degree of the crosslinking reaction between the epsilon-amino in the collagen solution with different concentrations and the aldehyde group in the OSA by adopting a TNBS method. The amount of reaction of epsilon-amino groups in collagen is proportional to the number of covalent crosslinks formed, i.e., the greater the amount of loss of epsilon-amino groups, the greater the number of covalent crosslinks formed. The results of the degree of crosslinking of the collagen gels of examples 1 to 3 are shown in FIG. 1, and it is understood from FIG. 1 that the absorbance values corresponding to the loss amount of the epsilon-amino group in the collagen gel samples modified by crosslinking are gradually increased under the condition of the same OSA content, that is, the degree of crosslinking of the collagen gel is increased as the concentration of the collagen solution is increased. The occurrence of this trend can be explained from two aspects: on the one hand, the increased concentration of collagen solution can provide more epsilon-amino groups to react with the aldehyde groups in OSA to form covalent crosslinks; on the other hand, the proportion of the ionic liquid in the two-phase solvent system is larger, so that the amount of hydrogen ions bonded to collagen molecules is reduced, and-NH is caused3 +The density of (a) is reduced, and the efficiency of the crosslinking reaction is improved to a certain extent.
Test examples
The collagen gel prepared in example 1 was used as a base material of a gel-type biosensor, the base material was made into a strip shape (convenient to be fixed with a finger), and the strip-shaped base material was connected to a three-electrode system of an electrochemical workstation, in which a reference electrode and a counter electrode were connected to one end of the strip-shaped base material, and a working electrode was connected to the other end of the strip-shaped base material. And after the i-t curve is stabilized, fixing the strip-shaped substrate material on the finger, and testing the resistance signal when the finger is bent, thereby realizing the collection of the resistance signal when the finger is bent by utilizing the electrochemical workstation. The impedance spectrogram of the detected electrochemical signal is shown in fig. 2, which shows that the collagen gel as the substrate material of the gel type biosensor can effectively identify the real-time feedback of the omnibearing information such as action amplitude, speed, frequency and the like.
The above description is only a preferred embodiment of the present invention and is not intended to limit the present invention, and various modifications and changes may be made by those skilled in the art. Any modification, equivalent replacement, or improvement made within the spirit and principle of the present invention should be included in the protection scope of the present invention.
Claims (10)
1. A method for preparing collagen gel is characterized in that freeze-dried collagen sponge is added into a polar solvent system to prepare a collagen solution, oxidized alginate is added into the collagen solution to carry out cross-linking reaction, and the collagen gel is obtained after the reaction; the polar solvent system is formed by blending ionic liquid and acetic acid aqueous solution.
2. The method for preparing collagen gel according to claim 1, wherein the polar solvent system has a pH of 1.5 to 5.0.
3. The method for preparing collagen gel according to claim 1, wherein said ionic liquid is one or more of 1-ethyl-3-methylimidazolyl acetate, 1-ethyl-3-methylimidazolyl formate, and 1-butyl-3-methylchloroimidazolyl acetate.
4. The method for preparing collagen gel according to claim 1, wherein the concentration of the acetic acid solution is 0.1 to 1.0 mol/L;
or the volume ratio of the ionic liquid to the acetic acid solution is 9: 1-5: 5.
5. The method for preparing a collagen gel according to claim 1, wherein the preparation of the collagen solution is carried out under ice-water bath conditions;
or the concentration of the collagen solution is 5-30 mg/mL.
6. The method for preparing collagen gel according to claim 1, wherein the time for the cross-linking reaction is 12 to 48 hours;
or the temperature of the crosslinking reaction is 2-10 ℃.
7. The method for preparing collagen gel according to claim 1, wherein said oxidized alginate is obtained by oxidizing alginate with an oxidizing agent;
preferably, the oxidizing agent is sodium periodate or potassium permanganate;
preferably, the mass ratio of the oxidant to the alginate is 1-2: 1;
preferably, the pH value of the system in the oxidation treatment process is 2-5;
preferably, the time of the oxidation treatment is 12-48 h.
8. A collagen gel obtained by the production method according to any one of claims 1 to 7.
9. Use of the collagen gel of claim 8 for the preparation of a biosensor.
10. A biosensor, wherein the collagen gel according to claim 8 is used as a base material.
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| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN115501391A (en) * | 2022-09-20 | 2022-12-23 | 浙江大学 | Collagen matrix flap with stable wet volume and preparation method thereof |
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| CN102351957A (en) * | 2011-08-18 | 2012-02-15 | 西南交通大学 | Oxidation method of natural polymeric amylose with high oxidisability |
| CN103418021A (en) * | 2013-08-08 | 2013-12-04 | 四川大学 | In-situ-crossly-linked electrospun fibrous membrane dressing made from collangen I and preparation method of in-situ crosslinking electrospun fibrous membrane dressing |
| CN105477678A (en) * | 2015-12-25 | 2016-04-13 | 四川大学 | Novel bio-medical adhesive and preparation method thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN102351957A (en) * | 2011-08-18 | 2012-02-15 | 西南交通大学 | Oxidation method of natural polymeric amylose with high oxidisability |
| CN103418021A (en) * | 2013-08-08 | 2013-12-04 | 四川大学 | In-situ-crossly-linked electrospun fibrous membrane dressing made from collangen I and preparation method of in-situ crosslinking electrospun fibrous membrane dressing |
| CN105477678A (en) * | 2015-12-25 | 2016-04-13 | 四川大学 | Novel bio-medical adhesive and preparation method thereof |
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| Publication number | Priority date | Publication date | Assignee | Title |
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| CN115501391A (en) * | 2022-09-20 | 2022-12-23 | 浙江大学 | Collagen matrix flap with stable wet volume and preparation method thereof |
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