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Temperature- and Photocontrolled Unfolding/Folding of a Triple-Helical Azobenzene-Stapled Collagen Peptide Monitored by Infrared Spectroscopy
- Source :
- Chemphyschem : a European journal of chemical physics and physical chemistry. 17(9)
- Publication Year :
- 2015
-
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.
- Subjects :
- Protein Denaturation
Protein Folding
Photoisomerization
Spectrophotometry, Infrared
Collagen helix
Infrared spectroscopy
Peptide
010402 general chemistry
01 natural sciences
chemistry.chemical_compound
Amino Acid Sequence
Physical and Theoretical Chemistry
chemistry.chemical_classification
010405 organic chemistry
Chemistry
Temperature
Atomic and Molecular Physics, and Optics
0104 chemical sciences
Crystallography
Azobenzene
Protein folding
Collagen
Peptides
Ethylene glycol
Azo Compounds
Triple helix
Subjects
Details
- ISSN :
- 14397641
- Volume :
- 17
- Issue :
- 9
- Database :
- OpenAIRE
- Journal :
- Chemphyschem : a European journal of chemical physics and physical chemistry
- Accession number :
- edsair.doi.dedup.....09ba3d95839f8de615503f23db57f3fb