Synthesis and biological applications of collagen-model triple-helical peptides

Org Biomol Chem. 2010 Mar 21;8(6):1237-58. doi: 10.1039/b920670a. Epub 2010 Jan 20.

Abstract

Triple-helical peptides (THPs) have been utilized as collagen models since the 1960s. The original focus for THP-based research was to unravel the structural determinants of collagen. In the last two decades, virtually all aspects of collagen structural biochemistry have been explored with THP models. More specifically, secondary amino acid analogs have been incorporated into THPs to more fully understand the forces that stabilize triple-helical structure. Heterotrimeric THPs have been utilized to better appreciate the contributions of chain sequence diversity on collagen function. The role of collagen as a cell signaling protein has been dissected using THPs that represent ligands for specific receptors. The mechanisms of collagenolysis have been investigated using THP substrates and inhibitors. Finally, THPs have been developed for biomaterial applications. These aspects of THP-based research are overviewed herein.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Biocompatible Materials / chemical synthesis*
  • Biocompatible Materials / chemistry
  • Biocompatible Materials / metabolism*
  • Collagen / chemistry*
  • Collagen / metabolism
  • Humans
  • Models, Molecular*
  • Molecular Sequence Data
  • Peptides / chemical synthesis*
  • Peptides / chemistry
  • Peptides / metabolism*
  • Protein Binding
  • Protein Stability
  • Protein Structure, Secondary

Substances

  • Biocompatible Materials
  • Peptides
  • Collagen