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A New Tool in Peptide Engineering: A Photoswitchable Stilbene‐type β‐Hairpin Mimetic
Author(s) -
Erdélyi Máté,
Karlén Anders,
Gogoll Adolf
Publication year - 2005
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.200500648
Subject(s) - photoisomerization , chemistry , circular dichroism , oligopeptide , peptide , chromophore , amide , helix (gastropod) , conformational change , stereochemistry , photochemistry , organic chemistry , isomerization , biochemistry , catalysis , ecology , snail , biology
Peptide secondary structure mimetics are important tools in medicinal chemistry, as they provide analogues of endogenous peptides with new physicochemical and pharmacological properties. The development, synthesis, photochemical investigation, and conformational analysis of a stilbene‐type β‐hairpin mimetic capable of light‐triggered conformational changes have been achieved. In addition to standard spectroscopic techniques (nuclear Overhauser effects, amide temperature coefficients, circular dichroism spectroscopy), the applicability of self‐diffusion measurements (longitudinal eddy current delay pulsed‐field gradient spin echo (LED‐PGSE) NMR technique) in conformational studies of oligopeptides is demonstrated. The title compound shows photoisomerization of the stilbene chromophore, resulting in a change in solution conformation between an unfolded structure and a folded β‐hairpin.