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Influence of different tripeptides on the stability of the collagen triple helix. II. An experimental approach with appropriate variations of a trimer model oligotripeptide
Author(s) -
Thakur S.,
Vadolas D.,
Germann H.P.,
Heidemann E.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250608
Subject(s) - tripeptide , chemistry , trimer , collagen helix , triple helix , peptide , stereochemistry , helix (gastropod) , covalent bond , circular dichroism , oligopeptide , crystallography , biochemistry , organic chemistry , dimer , ecology , snail , biology
A collagen model peptide comprising three covalently cross‐linked chains (Ala‐Gly‐Pro) 8 with a stable triple‐helix conformation was utilized as the constant part of elongated model peptides of different composition. The tripeptides Gly‐Pro‐Hyp, Gly‐Pro‐Ala, Gly‐Pro‐Pro, Gly‐Pro‐Ser, Gly‐Ala‐Hyp, Gly‐Phe‐Hyp, Gly‐Glu‐Hyp, Gly‐Ala‐Lys, and Gly‐Pro‐Phe were coupled at the N‐terminal to the cross‐linked peptide. The transition temperatures determined by CD measurements are higher for the peptides containing the Gly‐X‐Hyp sequences followed by those with the Gly‐Pro‐Y sequences. In experiments with combinations of two different tripeptides coupled to the constant part of the cross‐linked model peptides higher transition temperatures were observed if the sequence of helix‐promoting tripeptides was not interrupted.