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Updated: May 27, 2026
Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
Published on: January 31, 2014
A morphological and biochemical examination of the hydrothermal denaturation of collagen
1CSIRO Division of Food Research, PO Box 12, Cannon Hill, Queensland, Australia.
Abstract:
The morphological changes occurring during the hydrothermal denaturation of collagen obtained from the tendinous sheath of the longissimus dorsi muscle of mature sheep have been examined. To investigate the influence of the physical state of the collagen on its subsequent denaturation, collagen has been heated in the form of isolated fibrils, small pieces of unrestrained tissue and strips of tissue restrained from contracting fully during heating and cooling. The morphological changes occurring during denaturation and the thermal stability of the collagen to melting have been found to be dependent on the physical state of the collagen, the thermal stability of collagen being lowest in isolated fibrils, intermediate in unrestrained pieces, and highest in restrained samples. In conjunction with the morphological studies, the extent of dissolution of collagen by heat alone and the susceptibility of collagen to pronase digestion were measured and examined as possible biochemical criteria for assessing the extent of thermal denaturation of collagen.
