Biological and Rheological Properties of Collagen Cross-Linked with Glutaraldehyde
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MER MATERIALS FOR BIOMEDICINE
Biological and Rheological Properties of Collagen Cross-Linked with Glutaraldehyde Yu. A. Nashchekinaa,b,*, O. A. Lukoninaa, D. M. Darvisha, A. V. Nashchekinb, V. Yu. Elokhovskiic, V. E. Yudinc, and N. A. Mikhailovaa a Institute
of Cytology, Russian Academy of Sciences, St. Petersburg, 194064 Russia b Ioffe Institute, St. Petersburg, 194021 Russia c Peter the Great St. Petersburg Polytechnic University, St. Petersburg, 195251 Russia *e-mail: [email protected] Received January 29, 2020; revised January 29, 2020; accepted February 17, 2020
Abstract—We study the effect of the concentration of glutaraldehyde that can cross-link type I collagen molecules on the collagen stability, mechanical strength, and cytotoxicity. It is shown that collagen containing 10 and 18% of glutaraldehyde exhibits the highest stability in physiological conditions. The results of rheological analysis demonstrate that, for the minimal concentration of glutaraldehyde (1%), mechanical characteristics of collagen hydrogels are improved significantly. However, the glutaraldehyde concentration higher than 10% reduces the vitality of cells by 50%. DOI: 10.1134/S1063784220090224
INTRODUCTION Collagen is the most abundant protein in human tissues. At present, 28 types of collagen are known [1], which differ in the structure of the main polypeptide chain, in their localization in tissues, in executed functions, and so on. The most abundant protein in the organism is type I collagen that constitutes more than 90% of the organic mass of bones and the main component of tendons, skin, ligaments, cornea and many interarticular tissues except for hyaline cartilage, brain, and vitreous humor. The main function of collagen in the organism is the sustainment of structural integrity of tissues and organs. Among the modern technologies used in effective treatment of pathologies and in neogenesis of damaged tissues, cell technologies based on the transplantation of human cells on various carriers (scaffolds) play an important role [2]. The formation of such carriers based on the main structural element of connectives (namely, type I collagen) appears promising. During in vivo biosynthesis of collagen, transverse links formed between molecules impart a stabile structure, mechanical strength, and resistance to action of ferments to collagen fibrils. However, these links are broken during the separation of collagen from native tissues, and collagen loses its strength. The obtaining of mechanically strong gel by cross linking of collagen intended for producing scaffold and for cultivation and transplantation of cells is a topical problem in contemporary regenerative medicine.
At present, physical and chemical agents are used for cross-linking of collagen molecules. One chemical agent forming strong intermolecular cross links is glutaraldehyde (GA), which is a linear 5-carbon dialdehyde. Glutaraldehyde is widely used as a cross-linking agent for biomedical materials based on collagen [3, 4]. The mechanism of cross linking of collag
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