Thermal (in)stability of type I collagen fibrils

S.G. Gevorkian; A.E. Allahverdyan; D.S. Gevorgyan; A.L. Simonian

arXiv:0810.4172·cond-mat.soft·November 13, 2009

Thermal (in)stability of type I collagen fibrils

S.G. Gevorkian, A.E. Allahverdyan, D.S. Gevorgyan, A.L. Simonian

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TL;DR

This study investigates the temperature-dependent mechanical stability of rat collagen fibrils, revealing a complex five-stage mechanism that explains how collagen maintains stability at physiological temperatures despite inherent instability.

Contribution

It introduces a detailed five-stage mechanism explaining collagen fibril stability and instability across a broad temperature range, based on experimental measurements.

Findings

01

Young's modulus decreases at 25-45°C indicating instability

02

Maxima in hydration and damping at 70-80°C suggest structural changes

03

Heat denaturation at 120°C eliminates observed effects

Abstract

We measured Young's modulus at temperatures ranging from 20 to 100 ^{\circ} $C f or a co l l a g e n f ib r i l t ak e n f r o m r a t^{'} s t e n d o n . T h e h y d r a t i o n c han g e u n d er h e a t in g an d t h e d am p in g d ecr e m e n tw er e m e a s u r e d a s w e l l . A tp h y s i o l o g i c a l t e m p er a t u r es$ 25-45^{\circ} $C Y o u n g^{'} s m o d u l u s d ecr e a ses, w hi c h c anb e in t er p r e t e d a s in s t abi l i t y o f co l l a g e n . F or t e m p er a t u r es b e tw ee n$ 45-80^{\circ} $C Y o u n g^{'} s m o d u l u s f i r s t s t abi l i z es an d t h e nin cr e a ses w i t h d ecr e a s in g t h e t e m p er a t u r e . T h e h y d r a t e d w a t er co n t e n t an d t h e d am p in g d ecr e m e n t ha v es t r o n g ma x imain t h e in t er v a l$ 70-80^{\circ} $C in d i c a t in g o n co m pl e x in t er - m o l ec u l a r s t r u c t u r a l c han g es in t h e f ib r i l . A l l t h esee f f ec t s d i s a pp e a r a f t er h e a t - d e na t u r a t in g t h es am pl e a t$ 120^\circ$C. Our main result is a five-stage mechanism by which the instability of a single collagen at physiological temperatures is compensated by the interaction between collagen molecules…

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