Abstract
The triple-helical structure of a model collagen peptide possessing azobenzene-derived clamps integrated in all three strands as side-chain-to-side-chain crosslinks is analyzed by IR spectroscopy in comparative thermal excursion experiments with the triple helix of a typical reference collagen peptide consisting of only glycine-proline-hydroxyproline repeats. By exploiting the known stabilizing effects of aqueous alcoholic solvents on the unique collagen fold, deuterated ethylene glycol/water (1:1) is used as a solvent to investigate the effect of the light-switchable trans/cis-azobenzene clamp on the stability of the triple helix in terms of H/D exchange rates and thermal unfolding. Results of this comparative analysis clearly reveal only a minor destabilization of the triple helix by the hydrophobic azobenzene moieties compared to the reference collagen peptide as reflected by a lower midpoint of the thermal unfolding and higher rates of H/D exchange. However, it also reveals that the driving force exerted by the trans-to-cis photoisomerization of the azobenzene moieties is insufficient for unfolding of the compact triple-helical collagen fold. Only temperature-dependent untightening of this fold with heating results in a reversible photomodulated unfolding and refolding of the azo-collagen peptide into the original triple helix.
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