Application of collagen matrix as tissue engineering scaffold

A tissue engineering scaffold and collagen matrix technology, applied in medical science, prosthesis, etc., can solve the problems of poor mechanical properties and fast degradation, and achieve the effects of enhancing performance, improving flexibility, and increasing mechanical properties.

Inactive Publication Date: 2012-11-14
SANITARY EQUIP INST ACAD OF MILITARY MEDICAL SCI PLA
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

However, the use of sponges made of collagen alone as a scaffold material results in poor mechanical properties and rapid degradation

Method used

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  • Application of collagen matrix as tissue engineering scaffold
  • Application of collagen matrix as tissue engineering scaffold

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0045] Embodiment 1, preparation collagen matrix

[0046] (1) Producing collagen with the original tissue of animals, the specific steps are as follows:

[0047] 1. Remove collagen-rich isolated tissue (pig skin, cowhide, Achilles tendon, etc.) mechanically to remove impurities such as epidermis, muscle, and fat, and then wash it with tap water and pure water after crushing to obtain collagen tissue;

[0048] 2, the dilute alkali solution (mass and number ratio of preparation pH9.5, sodium hydroxide: sodium bicarbonate: water=0.5: 7.5: 92) and alcoholic substance aqueous solution (mass and number ratio, ethanol: Virahol: water =7:4:89);

[0049] 3. Wash the animal tissue obtained in the first step with the above prepared dilute alkali solution and aqueous alcohol solution in sequence to degrease it to obtain crude collagen;

[0050] 4. Dissolving the crude collagen product in a dilute formic acid solution with a pH of 6.0;

[0051]5. Add complex protease to the above soluti...

Embodiment 2

[0062] Embodiment 2, preparation collagen matrix

[0063] (1) Refining commercially available collagen, the specific steps are as follows:

[0064] 1. Dissolve commercially available collagen in dilute hydrochloric acid solution with pH 5.8;

[0065] 2, add composite protease in above-mentioned solution, the weight ratio of collagen and composite protease is 500: 1, and composite protease is made up of three kinds of proteases of activity ratio: pepsin: trypsin: papain=1: 1: 0.5, 34 Cultivate with stirring at ℃ for 11 hours;

[0066] 3. Centrifuge and collect the supernatant, add NaCl to the supernatant to make the concentration reach 2mol / L, stir at 8°C for 12 hours, and collect the obtained precipitate;

[0067] 4. Dissolve the precipitate in an aqueous solution of 0.3% acetic acid, and collect the supernatant by centrifugation;

[0068] 5. Add NaCl to the supernatant to make the concentration reach 1mol / L, and stir to obtain a precipitate; repeat the operation 4 times, a...

Embodiment 3

[0077] Embodiment 3, the enzymatic stability of collagen matrix

[0078] The rate of enzymatic degradation was determined by enzymatic degradation of collagen matrix.

[0079] The specific method is as follows: take fresh DMEM culture solution to prepare a collagenase solution with a concentration of 5 CDU / ml, and store it in cold storage; take a 5 mg collagen matrix sample, and package it with a plastic film 60 C 0 Sterilization; put the sample into 1ml type I collagenase solution, incubate at 37°C, replace the collagenase solution every day; take samples at 1h, 1.5h, 4h, 1d, 2d, 3d, 6d, 9d time points, each group 3 samples; add 200μl 0.25mol / L EDTA solution to the regularly sampled solution to terminate the digestion process; take out the sample with a small corner of the sample with tweezers, wash it with phosphate buffer (pH7.2) first, and then wash it with deionized water , placed in a clean small tube, and stored at -20°C for more than 24 hours; the sample was freeze-d...

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Abstract

The invention discloses novel application of a collagen matrix as a tissue engineering scaffold. The collagen matrix comprises the following substances expressed in mass parts: 50 to 90 of collagen, 8 to 48 of chitosan and 0.5 to 5 of glycerin. A preparation method for the collagen matrix comprises the following steps: 1) dissolving collagen in an acetic acid aqueous solution with a concentration of 0.01 to 0.1% to prepare a collagen solution with a concentration of 1 to 3%; 2) dissolving chitosan in the acetic acid aqueous solution with a concentration of 0.01 to 0.1% to prepare a chitosan solution with a concentration of 1 to 3%; 3) mixing the collagen solution, the chitosan solution (in terms of dry weight) and glycerin according to a mass ratio of 50-90: 8-48: 0.5-5 and carrying out freeze drying at a temperature of -80 DEG C to -10 DEG C for 1 to 5 d so as to obtain a spongy material; 4) immobilizing the spongy material with an aldehyde cross-linking agent at a temperature of 40 to 50 DEG C for 20 to 100 min; and 5) rinsing the spongy material with an aqueous solution of glycerin and drying the spongy material in vacuum so as to obtain the collagen matrix. According to results of cell culture experiments, the collagen matrix provided by the invention can promote cell growth and can be used as a tissue engineering scaffold.

Description

technical field [0001] The present invention relates to the application of collagen matrix as tissue engineering support material. Background technique [0002] Collagen is the most abundant protein in mammals. Its three-dimensional helical structure consists of three polypeptide chains. The repeating unit of the polypeptide chain is Gly-X-Y, and the X and Y positions are usually proline and 4-hydroxyproline. Collagen is readily purified from animal tissues such as skin, tendon, and discarded human tissues such as placenta. Collagen has the characteristics of low antigenicity, high affinity with cells, and hemagglutination with platelets, so it is widely used in the field of medicine. At least 27 genetically distinct collagen types have been identified. Taking type I collagen, which is the most abundant, as an example, about 95% of the collagen molecule is the domain of the three helical chains, and the remaining about 5% is the domain of the non-collagenous terminal pepti...

Claims

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Application Information

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Patent Type & Authority Applications(China)
IPC IPC(8): A61L27/26A61L27/20A61L27/24
Inventor 武继民张俊民郭涛李志宏张西正关静李瑞欣郭勇侍才洪黄姝杰
Owner SANITARY EQUIP INST ACAD OF MILITARY MEDICAL SCI PLA
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