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Solid-phase synthesis of triple-helical collagen-model peptides

✍ Scribed by Cynthia G. Fields; Beate Grab; Janelle L. Lauer; Andrew J. Miles; Ying-Ching Yu; Gregg B. Fields

Book ID
104634218
Publisher
Springer Netherlands
Year
1996
Tongue
English
Weight
803 KB
Volume
3
Category
Article
ISSN
1573-3149

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✦ Synopsis

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. *This paper is based on a presentation given at the Symposium on Peptide Structure and Design as part of the

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