The Renaturation Behaviour of Modified Collagen Molecules

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Abstract
The step that is most difficult to understand in the renaturation of collagen molecules is how the pep-tide chains find the correct register to one another necessary to construct the native triple-helix. The aim of this investigation was to establish whether electrostatic interactions contribute to the regulation of this process. The charge pattern of the molecules was varied by chemically altering the amino acid side chains. The thermal stability of these derivatives of acid soluble collagen is variously reduced. Their ability to reform molecules with native structure after denaturation was investigated at 2 different pH values (3.7 and 7.4). No direct correlation could be recognized between the change in the charge pattern and the renaturation behavior. This excludes the possibility of the regulating function of electrostatic forces in the aligning of the peptide chains. There is however a close relationship between the stability of the native molecule and its reformation after denaturation. The results suggest that the alignment of the peptide chains during the reformation of collagen molecules is mainly regulated by the stability of the resulting structures.