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Stronger and Longer Synthetic Collagen

Published online by Cambridge University Press:  01 February 2011

Ronald T. Raines
Ronald T. Raines*
Affiliation:
rtraines@wisc.edu, University of Wisconsin-Madison, Department of Biochemistry, 433 Babcock Drive, Madison, WI, 53706-1544, United States, 608-262-8588, 608-262-3453
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Abstract

Collagen is the most abundant protein in the human proteome. The post-translational modification of collagen by the enzyme prolyl 4-hydroxylase increases markedly the conformational stability of the collagen triple helix. We have discovered that a previously unappreciated force—stereoelectronic effects—is responsible for this increased stability. By exploiting these stereoelectronic effects (e.g., the gauche effect and n→π* interaction) and reciprocal steric effects, we have created synthetic collagen of unprecedented stability. We have also used the molecular self-assembly of triple-helical fragments to create synthetic collagen of unprecedented length. These synthetic collagens have numerous applications in biotechnology and biomedicine.

Keywords

biological synthesis (assembly)biomaterialbiomedical
Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 1062: Symposium NN – Protein and Peptide Engineering for Therapeutic and Functional Materials , 2007 , 1062-NN01-02-MM01-02
Copyright
Copyright © Materials Research Society 2008

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