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Perspectives on the synthesis and application of triple‐helical, collagen‐model peptides
Author(s) -
Fields Gregg B.,
Prockop Darwin J.
Publication year - 1996
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1996)40:4<345::aid-bip1>3.0.co;2-w
Subject(s) - chemistry , triple helix , collagen helix , combinatorial chemistry , stereochemistry
Collagens can be distinguished from other proteins based on their triple‐helical structure. Synthetic peptide models have been developed to better understand the triple helix structurally and to evaluate the triple helix as a recognition element for biological processes. Associated triple‐helical peptides were first designed and assembled by solid‐phase methodology in the late 1960s. Such peptides were used for triple‐helical structural characterization by CD, nmr, and ir spectroscopies, and x‐ray crystallography, and for studying the structural preferences of hydroxylases. In the late 1970s, methods were developed for covalently linking the three strands of triple‐helical peptides. One benefit of “branched” peptides was the enhancement of triple‐helical thermal stability. The incorporation of specific collagen sequences into thermally stable synthetic triple helices in the early 1990s has allowed for the mechanistic investigation of collagen‐mediated cell adhesion and platelet aggregation. In time, discriminatory therapeutics may result from the continued exploration and further understanding of the biological effects of collagen primary, secondary, and tertiary structures via triple‐helical peptide models. © 1996 John Wiley & Sons, Inc.