Link-lock: An explanation of the chemical stabilisation of collagen

TY - JOUR

T1 - Link-lock

T2 - An explanation of the chemical stabilisation of collagen

AU - Covington, A. D.

AU - Song, L.

AU - Suparno, O.

AU - Koon, H. E. C.

AU - Collins, M. J.

PY - 2008/1

Y1 - 2008/1

N2 - Chemical modifications of collagen, of the type known in the leather tanning industry, can raise the denaturation temperature, from 60 degrees C in its natural state, up to 130 degrees C. There are only a few chemical reactions known to be capable of achieving the highest values and these have long been assumed to be unrelated. Here, we show for the first time that all the stabilising mechanisms are fundamentally the same, regardless of chemical type. Any single component of a stabilising reaction has the effect of linking part of the collagen structure into the surrounding matrix of water: the outcome is always to confer moderate hydrothermal stability, up to 85 degrees C. The effect is merely to hinder the shrinking/denaturation transition, so no single component reaction can exceed this moderate result. However, in addition, a second reaction component can be applied in the process, which may have the ability to lock the linked structure together, creating a macromolecular structure around the triple helices. The effect of the concerted interaction with collagen is to prevent more effectively the unravelling of the triple helices and thereby to raise the hydrothermal stability to much higher values of denaturation temperature. This new proposed 'link-lock' mechanism opens up the possibility of achieving high collagen stability in new ways, which will contribute to the development of new collagenic biomaterials.

AB - Chemical modifications of collagen, of the type known in the leather tanning industry, can raise the denaturation temperature, from 60 degrees C in its natural state, up to 130 degrees C. There are only a few chemical reactions known to be capable of achieving the highest values and these have long been assumed to be unrelated. Here, we show for the first time that all the stabilising mechanisms are fundamentally the same, regardless of chemical type. Any single component of a stabilising reaction has the effect of linking part of the collagen structure into the surrounding matrix of water: the outcome is always to confer moderate hydrothermal stability, up to 85 degrees C. The effect is merely to hinder the shrinking/denaturation transition, so no single component reaction can exceed this moderate result. However, in addition, a second reaction component can be applied in the process, which may have the ability to lock the linked structure together, creating a macromolecular structure around the triple helices. The effect of the concerted interaction with collagen is to prevent more effectively the unravelling of the triple helices and thereby to raise the hydrothermal stability to much higher values of denaturation temperature. This new proposed 'link-lock' mechanism opens up the possibility of achieving high collagen stability in new ways, which will contribute to the development of new collagenic biomaterials.

KW - THERMAL STABILIZATION

KW - VEGETABLE TANNINS

KW - PART 1

KW - STABILITY

KW - POLYPHENOLS

KW - FIBERS

KW - DENATURATION

KW - DEGRADATION

KW - MOLECULES

KW - MECHANISM

UR - http://www.scopus.com/inward/record.url?scp=39549105170&partnerID=8YFLogxK

M3 - Article

SN - 0144-0322

VL - 92

SP - 17

JO - Journal of the society of leather technologists and chemists

JF - Journal of the society of leather technologists and chemists

IS - 1

ER -