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A synthetic model of collagen: An experimental investigation of the triple-helix stability

✍ Scribed by H.-P. Germann; E. Heidemann

Publisher
Wiley (John Wiley & Sons)
Year
1988
Tongue
English
Weight
367 KB
Volume
27
Category
Article
ISSN
0006-3525

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✦ Synopsis

Synopsis

Variations I-XVIII of a trimerlike cross-linked collagen model peptide were synthesized and used to investigate the cooperation of different neighboring Gly-X-Y tripeptides. The carboxyterminal decapentapeptide of the triple-helical part of collagen type I was chosen as the starting point of sequentially modified elongations. The transition temperatures determined by CD measurements show that the incorporation of the imino acid free tripeptides Gly-Ala-Ala and Gly-Ile-Ala results in a weakening of the triple-helical structure. I t is demonstrated that the desired thermal stability of the collagen triple helix requires the "clustered" arrangement of helix-promoting tripeptides, especially of Gly-Pro-Hyp.

πŸ“œ SIMILAR VOLUMES

Influence of different tripeptides on th
Influence of different tripeptides on the stability of the collagen triple helix. II. An experimental approach with appropriate variations of a trimer model oligotripeptide
✍ S. Thakur; D. Vadolas; H.-P. Germann; E. Heidemann πŸ“‚ Article πŸ“… 1986 πŸ› Wiley (John Wiley & Sons) 🌐 English βš– 295 KB

A collagen model peptide comprising three covalently cross-linked chains (Ala-Gly-ProIg with a stable triple-helix conformation was utilized as the constant part of elongated model peptides of different composition.