Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Binding Sites
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Biochemistry / methods
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Carbamates / chemistry*
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Carbamates / metabolism
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Carbamates / pharmacology*
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Chymotrypsin / antagonists & inhibitors*
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Chymotrypsin / metabolism
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Drug Evaluation, Preclinical
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Peptides / chemistry
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Peptides / pharmacology
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Phenylalanine / analogs & derivatives
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Phenylalanine / chemistry*
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Phenylalanine / metabolism
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Phenylalanine / pharmacology*
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Photochemistry / methods*
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Serine Proteinase Inhibitors / chemistry*
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Serine Proteinase Inhibitors / metabolism
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Serine Proteinase Inhibitors / pharmacology*
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Structure-Activity Relationship
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Ultraviolet Rays
Substances
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Carbamates
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Peptides
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Serine Proteinase Inhibitors
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azobenzene carbamate-phenylalanine
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Phenylalanine
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Chymotrypsin
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alpha-chymotrypsin