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Improved Photocontrol of α‐Chymotrypsin Activity: Peptidomimetic Trifluoromethylketone Photoswitch Enzyme Inhibitors
Author(s) -
Pearson David,
Alexander Nathan,
Abell Andrew D.
Publication year - 2008
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.200800082
Subject(s) - peptidomimetic , photoswitch , chymotrypsin , azobenzene , chemistry , enzyme , stereochemistry , serine protease , protease , serine , biochemistry , trypsin , peptide , organic chemistry , molecule
A series of peptidomimetic trifluoromethylketones containing the photoisomerisable azobenzene group have been synthesised, photoisomerised and assayed against the serine protease α‐chymotrypsin. All are inhibitors of the enzyme and exhibit up to a fivefold increase in activity on UV irradiation. Visible irradiation returns activity to close to that of the original sample. These results suggest the trifluoromethylketone group to be the best electrophilic enzyme binding group for use in photoswitch inhibitors of α‐chymotrypsin.