Alpha-ketoester-based photobiological switches: synthesis, peptide chain extension and assay against alpha-chymotrypsin.
The design, synthesis, photoisomerism and biological testing of two peptide-based photoswitchable inhibitors of alpha-chymotrypsin are presented. The use of a dipeptide recognition sequence gave a 'slow-tight binding' inhibitor, while the introduction of a carbamate linker to the azobenzene gave a modest enhancement in photoswitching of enzyme activity for the photostationary state enriched in the (Z)-isomer over the (E)-isomer.
Harvey
A J
AJ
Department of Chemistry, University of Canterbury, Christchurch, New Zealand.
Abell
A D
AD
D001665:Binding Sites; D001671:Biochemistry / Q000379:methods; D002219:Carbamates / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D002918:Chymotrypsin / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004353:Drug Evaluation, Preclinical; D010455:Peptides / Q000737:chemistry / Q000494:pharmacology; D010649:Phenylalanine / Q000031:analogs & derivatives / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D010777:Photochemistry / Q000379:methods*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D013329:Structure-Activity Relationship; D014466:Ultraviolet Rays
D002219:Carbamates; D010455:Peptides; D015842:Serine Proteinase Inhibitors; C448388:azobenzene carbamate-phenylalanine; D010649:Phenylalanine; D002918:Chymotrypsin; C117608:alpha-chymotrypsin