Thermally Labile Cross-links in Native Collagen

Abstract

AN outstanding characteristic of the collagen fibre is the sharp contraction to about one-third of its initial length on heating^1,2. The generally accepted view is that melting involves the rupture of secondary valence bonds and a rearrangement of the triple helical structure into a random configuration³, the stable covalent inter and intramolecular bonds remaining intact⁴. We now propose that a proportion of the covalent intermolecular cross-links present in native collagen are thermally labile and are also ruptured during the shrinkage process.