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Stabilization of collagen through bioconversion: An insight in protein–protein interaction
Article first published online: 26 MAY 2014
© 2014 Wiley Periodicals, Inc.
Volume 101, Issue 8, pages 903–911, August 2014
How to Cite
Usharani, N., Jayakumar, G. C., Kanth, S. V., Rao, J. R. (2014), Stabilization of collagen through bioconversion: An insight in protein–protein interaction. Biopolymers, 101: 903–911. doi: 10.1002/bip.22473
- Issue published online: 26 MAY 2014
- Article first published online: 26 MAY 2014
- Accepted manuscript online: 15 FEB 2014 02:12PM EST
- Manuscript Accepted: 13 JAN 2014
- Manuscript Revised: 8 JAN 2014
- Manuscript Received: 3 OCT 2013
- aldehyde forming enzyme;
- denaturation temperature;
Collagen is a natural protein, which is used as a vital biomaterial in tissue engineering. The major concern about native collagen is lack of its thermal stability and weak resistance to proteolytic degradation. In this scenario, the crosslinking compounds used for stabilization of collagen are mostly of chemical nature and exhibit toxicity. The enzyme mediated crosslinking of collagen provides a novel alternative, nontoxic method for stabilization. In this study, aldehyde forming enzyme (AFE) is used in the bioconversion of hydroxylmethyl groups of collagen to formyl groups that results in the formation of peptidyl aldehyde. The resulted peptidyl aldehyde interacts with bipolar ions of basic amino acid residues of collagen. Further interaction leads to the formation of conjugated double bonds (aldol condensation involving the aldehyde group of peptidyl aldehyde) within the collagen. The enzyme modified collagen matrices have shown an increase in the denaturation temperature, when compared with native collagen. Enzyme modified collagen membranes exhibit resistance toward collagenolytic activity. Moreover, they exhibited a nontoxic nature. The catalytic activity of AFE on collagen as a substrate establishes an efficient modification, which enhances the structural stability of collagen. This finds new avenues in the context of protein–protein stabilization and discovers paramount application in tissue engineering. © 2014 Wiley Periodicals, Inc. Biopolymers 101: 903–911, 2014.