The hydrophobic effect and hydrogen bonding have long been known to direct a polypeptide chain to assume a folded structure. Using synthetic peptides, we have shown that a previously unappreciated force�stereoelectronic effects�is responsible for the increased stability endowed upon the collagen triple helix by its prevalent 4-hydroxyproline residues. Exploiting these stereoelectronic effects (along with reciprocal steric effects and molecular self-assembly) has enabled us to create synthetic collagens of unprecedented length and stability. We are using such peptidic materials as the core of nanowires and as pylons for pendant growth factors that promote the healing of wounds in mice.

Longer, stronger synthetic collagens for nanotechnology and biomedicine

245th National Meeting (2013)

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