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Medical grade reconstructed collagen cross-linking modified method

A collagen cross-linking and cross-linking modification technology, applied in medical science, prostheses, etc., can solve the problems of cytotoxicity and difficult-to-control degradation, achieve easy cross-linking, improve mechanical properties, and control cross-linking Effect

Inactive Publication Date: 2011-04-20
SICHUAN UNIV
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

Common chemical cross-linking methods are cytotoxic, and physical cross-linking methods are difficult to control its degradation

Method used

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  • Medical grade reconstructed collagen cross-linking modified method
  • Medical grade reconstructed collagen cross-linking modified method
  • Medical grade reconstructed collagen cross-linking modified method

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0032] Add 1ml of potassium phosphate solution with a concentration of 0.1mol / L to 5ml of uniform collagen solution with a concentration of 5mg / ml at a temperature of 15°C and slowly stir, adjust the pH of the mixed solution to 7.0 with an acid or alkali solution, and mix The solution is kept at a temperature of 25°C and a humidity of 50%, and it is allowed to stand for 6 hours to make it into a uniform colloid. After the colloid is placed in an environment of -20°C and -60°C for 24 hours, it is dehydrated in a freeze dryer to obtain ions Crosslinked Modified Reconstituted Collagen.

Embodiment 2

[0034] Add 5ml of sodium phosphate solution with a concentration of 0.5mol / L to 25ml of a uniform normal collagen solution with a concentration of 10mg / ml at a temperature of 20°C and slowly stir, adjust the pH of the mixed solution to 8.5 with an acid or alkali solution, and mix The solution is kept at a temperature of 40°C and a humidity of 70%, and it is allowed to stand for 12 hours to make it into a uniform colloid. After the colloid is placed in an environment of -40°C and -80°C for 48 hours, it is dehydrated in a freeze dryer to obtain ions Crosslinked Modified Reconstituted Collagen.

Embodiment 3

[0036] Add 2ml of dipotassium hydrogen phosphate solution with a concentration of 0.2mol / L to 10ml of ordinary collagen solution with a uniform concentration of 6mg / ml at a temperature of 16°C and slowly stir, and adjust the pH value of the mixed solution to 7.2 with acid or alkali solution , the mixed solution is kept at a temperature of 28°C and a humidity of 55%, and it is left to stand for 8 hours to make it into a uniform colloid. Obtain ionically cross-linked modified collagen.

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Abstract

The invention discloses a method for cross-linking and modifying medical-grade reconstructed collagen, which is characterized in that 1 to 5 weight parts of phosphate solution with the concentration of 0.1 mol / L to 0.5mol / L is added into 5 to 25 weight parts of uniform regular collagen solution with the concentration of 5 mg / ml to 10mg / ml at the temperature of 15 DEG C to 20 DEG C while slowly stirring. Acid solution or aqueous alkali is used for adjusting the pH value of the mixed solution to 7.0 to 8.5. The mixed solution stands for 6 hours to 12 hours at the temperature of 25 DEG C to 40 DEG C and humidity of 50 percent to 70 percent so as to form uniform colloid. The colloid is sequentially arranged in the environment of minus 20 DEG C to minus 40 DEG C and minus 60 DEG C to minus 80 DEG C to be frozen for 24 hours to 48 hours, and then dehydrated in a lyophilizer to obtain the reconstructed collagen with cross-linked and modified ions.

Description

technical field [0001] The invention relates to a method for cross-linking modification of medical-grade reconstructed collagen, which belongs to the field of biomedical material preparation. Background technique [0002] Collagen is the basic structural material of vertebrates, the most abundant protein in mammals, and the main protein that constitutes animal connective tissue. It accounts for about 1 / 3 of the total protein in vertebrates, and mainly exists in bones, skin and tendons. Type I collagen, also known as tropocollagen, has a rod-shaped molecule with a length of about 300nm, a diameter of about 1.5nm, and a molecular weight of about 300,000. Its basic structure is a three-strand chain, consisting of two α1(I) and one α2 (1) Chain composition, each α-chain contains 1056 amino acid residues, and the three α-chains are in a right-handed manner, winding each other into three superhelical strands. In fact, all different types of collagen are formed in the form of tri...

Claims

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Application Information

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Patent Type & Authority Patents(China)
IPC IPC(8): C08J3/24C08L89/00C08K3/32A61L27/24
Inventor 蒋波张焰鲁建魏清荣
Owner SICHUAN UNIV
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