glycyl-prolyl-hydroxyproline and azobenzene

glycyl-prolyl-hydroxyproline has been researched along with azobenzene* in 1 studies

Other Studies

1 other study(ies) available for glycyl-prolyl-hydroxyproline and azobenzene

ArticleYear
Photocontrol of the collagen triple helix: synthesis and conformational characterization of bis-cysteinyl collagenous peptides with an azobenzene clamp.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2007, Volume: 13, Issue:10

    For the photomodulation of the collagen triple helix with an azobenzene clamp, we investigated various collagenous peptides consisting of ideal (Gly-Pro-Hyp) repeats and containing cysteine residues in various positions for a side chain-to-side chain crosslink with a suitable chromophore derivative. Comparative conformational analysis of these cysteine peptides indicated an undecarepeat peptide with two cysteine residues located in the central portion in i and i+7 positions and flanked by (Gly-Pro-Hyp) repeat sequences as the most promising for the cross-bridging experiments. In aqueous alcoholic solution the azobenzene-undecarepeat peptide formed a stable triple helix in equilibrium with the monomeric species as a trans-azobenzene isomer, whereas photoisomerization to the cis isomer leads to unfolding of at least part of the triple helix. Furthermore, the residual supercoiled structure acts like an intermolecular knot, thus making refolding upon cis-to-trans isomerization a concentration-independent fast event. Consequently, these photoswitchable collagenous systems should be well suited for time-resolved studies of folding/unfolding of the collagen triple helix under variable thermodynamic equilibria.

    Topics: Amino Acid Sequence; Azo Compounds; Circular Dichroism; Collagen; Cysteine; Isomerism; Magnetic Resonance Spectroscopy; Molecular Sequence Data; Oligopeptides; Peptides; Photochemistry; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Solutions; Temperature; Time Factors

2007