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.
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Raines, R.T. Stronger and Longer Synthetic Collagen. MRS Online Proceedings Library 1062, 1020102 (2007). https://doi.org/10.1557/PROC-1062-NN01-02-MM01-02
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DOI: https://doi.org/10.1557/PROC-1062-NN01-02-MM01-02