Composite crosslinked type I collagen membrane and preparation method thereof

Abstract

The invention discloses a preparation method of a composite crosslinked type I collagen membrane. The method includes the steps of: firstly subjecting type I collagen to dissolution stirring in an acid solution in a reaction kettle for 12-24h, then adding a defoaming agent into the solution, conducting stirring for 20-60min, then pumping the solution into a storage tank, and conducting static defoaming; conducting inspection to ensure that defoaming reaches the requirement, then pumping the solution into a film casting machine, carrying out film casting, then performing drying, dipping the film into a first cross-linking agent solution or placing the film under cross-linking conditions for 12-24h, and conducting cleaning, then dipping the film into a second cross-linking agent solution or placing the film under cross-linking conditions for 12-24h, and then performing cleaning and drying; and finally, conducting forming processing, packaging and irradiation, thus obtaining the composite crosslinked type I collagen membrane. The membrane material has good mechanical properties, hydrophilicity, antimicrobial activity and biological compatibility, the degradation rate is controllable and can reach long degradation time, also the preparation process is simple, the equipment is simple, the raw materials are cheap and easily available, and the composite crosslinked type I collagen membrane can be widely used as medical wound dressings, tissue engineering scaffold materials and the like in the medical field.

Description

technical field [0001] The invention relates to a composite crosslinked type I collagen film and a preparation method thereof, belonging to the field of biomedical materials. Background technique [0002] Collagen is a natural protein with a wide range of sources. It mainly exists in animal skin, bone, Achilles tendon, ligament and blood vessel. It is an important structural protein in connective tissue and cartilage tissue. The most studied one is mainly type I collagen. Compared with other proteins, type I collagen has better biological activity, can promote cell proliferation, growth, differentiation and migration, is biodegradable and has good tissue compatibility. However, the mechanical properties and enzymolysis resistance of collagen materials are limited, thus limiting their application in the field of biomedical materials. The modification and cross-linking of collagen materials can obviously improve its shortcomings. Proanthocyanidin is a plant polyphenol with ...

AI Technical Summary

Problems solved by technology

[0004] In the above method, there are the following deficiencies: (1) Most of the collagen raw material (collagen) is a hydrolyzed product of collagen, which has lost the unique biological activity when collagen maintains a triple helix, and some properties have been lost; (2) The toxicity of the cross-linking agent itself is relatively high. (3) The cross-linking degree of the material is not high, and the mechanical properties and enzymolysis resistance cannot be greatly improved; (4) The cross-linking agent itself does not have beneficial properties. function, it cannot endow the collagen membrane material with new and more excellent properties while modifying