For clinical treatments where exogenous collagen is introduced into the body, resistance to degradation is desired. Recent studies have shown that replacing glycine in a Pro-Hyp-Gly repeat unit with azaglycine significantly raises the Tm of the triple helix. We are exploring a different approach to stabilizing collagen. Instead of modifying the amino acid residues themselves, we have anchored the N-termini of ~20-residue collagen peptides to a luminescent Ru(II) metal ion. Much like how a shoelace is prevented from fraying by an aglet, metal binding should discourage helix unwinding. The resultant complexes are water-soluble and easily purified by reversed-phase HPLC. Temperature-dependent CD spectroscopy and NMR have been used to examine the effects of installing a flexible linker between the metal ion “hub” and the individual strands, thus allowing the peptides to approach each other in a manner that favors strong interactions.

Stabilizing the collagen triple helix with a ruthenium(II) anchor

253rd National Meeting (2017)

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