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Synthesis of heterotrimeric collagen peptides containing the α1β1 integrin recognition site of collagen type IV
Author(s) -
Saccá Barbara,
Moroder Luis
Publication year - 2002
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.385
Subject(s) - heterotrimeric g protein , integrin , chemistry , collagen receptor , collagen, type i, alpha 1 , epitope , type i collagen , type iv collagen , basement membrane , structural motif , peptide , biochemistry , microbiology and biotechnology , stereochemistry , biophysics , cell , laminin , biology , antibody , immunology , signal transduction , extracellular matrix , g protein , endocrinology
Collagen type IV provides a biomechanically stable scaffold into which the other constituents of basement membranes are incorporated, but it also plays an important role in cell adhesion. This occurs with collagen type IV mainly via the α1β1 integrin, and the proposed epitope involved in this type of collagen/integrin interaction corresponds to a non‐sequential R/Xaa/D motif, where the arginine and aspartate residues are provided by the α2 and α1 chains of the collagen molecule, respectively. Since the stagger of the three α chains in native collagen type IV is still unknown and different alignments of the chains lead to different spatial epitopes, two heterotrimeric collagen peptides containing the natural 457–469 sequences of the cell adhesion site were synthesized in which the single chains were assembled via disulfide bonds into the two most plausible α1α2α1′ and α2α1α1′ registers. The differentiated triple‐helical stabilities of the two heterotrimers suggest a significant structural role of the chain register in collagen, although the binding to α1β1 integrin is apparently less affected as indicated by preliminary experiments. Copyright © 2002 European Peptide Society and John Wiley & Sons, Ltd.