Perspectives on the synthesis and application of triple-helical, collagen-model peptides.
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.
Fields
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GB
Department of Laboratory Medicine, University of Minnesota, Minneapolis 55455, USA.
Prockop
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DJ
D000595:Amino Acid Sequence; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis*; D017433:Protein Structure, Secondary
D010455:Peptides