The dissection of the activities mediated by type I collagen requires an approach by which the influence of triple-helical conformation can be evaluated. The ␣ 1 ␤ 1 and ␣ 2 ␤ 1 integrin binding sites within type I collagen are dependent upon triple-helical conformation and contained within residues 124 -822 from ␣1(I). Seven

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The triple-helical conformation of collagen has been proposed to be important for mediation of cellular activities, such as adhesion and activation, extracellular matrix assembly, and enzyme function. We have developed synthetic protocols that allow for the study of biological activities of specific collagen sequences in triple-helical conformation. These methods primarily involve solid-phase assembly and covalent linkage of three peptide chains. The resultant triple-helical peptides have sufficient thermal stabilities to permit structural and biological characterization under physiological conditions. The present article critically reviews the various approaches for constructing synthetic triple-helices.

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