Is dialdehyde starch a valuable cross-linking agent for collagen/elastin based materials?

Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical support, strength, and elasticity to various organs and tissues, e.g. skin, tendons, arteries, and bones. They are readily available, biodegradable, biocompatible and they stimulate cell growth. The physi...

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Published inJournal of materials science. Materials in medicine Vol. 27; no. 4; pp. 67 - 10
Main Authors Skopinska-Wisniewska, J., Wegrzynowska-Drzymalska, K., Bajek, A., Maj, M., Sionkowska, A.
Format Journal Article
LanguageEnglish
Published New York Springer US 01.04.2016
Springer Nature B.V
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Summary:Collagen and elastin are the main structural proteins in mammal bodies. They provide mechanical support, strength, and elasticity to various organs and tissues, e.g. skin, tendons, arteries, and bones. They are readily available, biodegradable, biocompatible and they stimulate cell growth. The physicochemical properties of collagen and elastin-based materials can be modified by cross-linking. Glutaraldehyde is one of the most efficient cross-linking agents. However, the unreacted molecules can be released from the material and cause cytotoxic reactions. Thus, the aim of our work was to investigate the influence of a safer, macromolecular cross-linking agent—dialdehyde starch (DAS). The properties of hydrogels based on collagen/elastin mixtures (95/5, 90/10) containing 5 and 10 % of DAS and neutralized via dialysis against deionized water were tested. The homogenous, transparent, stiff hydrogels were obtained. The DAS addition causes the formation of intermolecular cross-linking bonds but does not affect the secondary structure of the proteins. As a result, the thermal stability, mechanical strength, and, surprisingly, swelling ability increased. At the same time, the surface properties test and in vitro study show that the materials are attractive for 3T3 cells. Moreover, the materials containing 10 % of DAS are more resistant to enzymatic degradation.
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ISSN:0957-4530
1573-4838
DOI:10.1007/s10856-016-5677-6