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Interaction of aldehydes with collagen: effect on thermal, enzymatic and conformational stability.

Abstract：

:Stabilization of type I rat tail tendon (RTT) collagen by various aldehydes, viz. formaldehyde, gluteraldehyde, glyoxal and crotanaldehyde was studied to understand the effect of each on the thermal, enzymatic and conformational stability of collagen. The aldehydes have been found to increase the heat stability of rat tail tendon collagen fibres from 62 to 77-86 degrees C. The increase in thermal stability was found to be in a species dependent manner. The variation in the thermal stability of collagen brought about by aldehydes was in the order of formaldehyde > gluteraldehyde > glyoxal > crotanaldehdye. The aldehydes also impart a high degree of stability to collagen against the activity of the degrading enzyme, collagenase. The order of enzymatic stability brought about by aldehydes follows the same trend as the thermal stability brought about by them. This shows that the number of cross-links formed influence both the thermal and enzymatic stability in the similar manner. The effect of various aldehydes on the secondary structure of collagen was studied using circular dichroism and it was found that the aldehydes lead to changes in the amplitude of the circular dichroic (CD) spectrum but did not alter the triple helical conformation of collagen. The secondary structure of collagen is not significantly altered on interaction with different aldehydes.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Fathima NN,Madhan B,Rao JR,Nair BU,Ramasami T

doi

10.1016/j.ijbiomac.2004.05.004

keywords:

subject

Has Abstract

pub_date

2004-08-01 00:00:00

pages

241-7

issue

4

eissn

0141-8130

issn

1879-0003

pii

S0141813004000376

journal_volume

34

pub_type

杂志文章

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