The properties conferred upon triple-helical collagen-mimetic peptides by the presence of cysteine residues.

Peptides
D A SlatterRichard W Farndale

Abstract

Recently, the ability of polymeric collagen-like peptides to regulate cell behavior has generated great interest. A triple-helical peptide known as collagen-related peptide (CRP) contains the sequence (Gly-Pro-Hyp)(10). With Gly-Pro-Cys triplets appended to both of its termini, designated CRP(cys), chemical cross-linking using heterobifunctional reagents generates CRP(cys)-XL, a potent, widely used, polymeric agonist for platelet Glycoprotein VI, whereas non-cross-linked, monomeric CRP(cys) antagonizes Glycoprotein VI. Here, we describe how cysteine in these triplets may also undergo random air-induced oxidation, especially upon prolonged storage or repeated freeze-thawing, to form disulphide bonds, resulting in a lesser degree of polymerization than with chemical cross-linking. We investigated the monomeric and polymeric states of these and other cysteine-containing collagen-derived peptides, using gel filtration and dynamic light scattering, allowing the size of a CRP-XL aggregate to be estimated. The effect of cysteine thiols upon peptide adsorption to surfaces and subsequent platelet responses was investigated. This demonstrated that cysteine is required for strong binding to glass coverslips and to plastic plates used in E...Continue Reading

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Citations

Dec 4, 2015·Advanced Drug Delivery Reviews·Bo AnBarbara Brodsky
Jul 4, 2019·Essays in Biochemistry·Richard W Farndale
Jul 11, 2014·The Journal of Biological Chemistry·Joanna-Marie HowesRichard W Farndale
Oct 12, 2015·ACS Biomaterials Science & Engineering·Jeremy Gleaton, Jean Chmielewski
Aug 28, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Jeremy GleatonJean Chmielewski

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