Diarylethene‐Based Photoswitchable Inhibitors of Serine Proteases

A bicyclic peptide scaffold was chemically adapted to generate diarylethene‐based photoswitchable inhibitors of serine protease Bos taurus trypsin 1 (T1). Starting from a prototype molecule—sunflower trypsin inhibitor‐1 (SFTI‐1)—we obtained light‐controllable inhibitors of T1 with Ki in the low nano...

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Veröffentlicht in:	Angewandte Chemie International Edition 2021-09, Vol.60 (40), p.21789-21794
Hauptverfasser:	Babii, Oleg, Afonin, Sergii, Diel, Christian, Huhn, Marcel, Dommermuth, Jennifer, Schober, Tim, Koniev, Serhii, Hrebonkin, Andrii, Nesterov‐Mueller, Alexander, Komarov, Igor V., Ulrich, Anne S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antiinfectives and antibacterials Antimicrobial peptides bicyclic peptide Cattle Communication Communications diarylethene photoswitch Enzymatic activity Enzyme activity Enzymes Ethylenes - chemistry Ethylenes - pharmacology Gelatin hydrogel photoregulation Hydrogels Hydrogen bonds Irradiation Isomerization Molecular Structure Peptides Peptides, Cyclic - chemistry Peptides, Cyclic - pharmacology Protease Protease inhibitors Proteinase inhibitors Proteolysis Radiation Serine serine protease inhibitors Serine Proteases - metabolism Serine proteinase Serine Proteinase Inhibitors - chemistry Serine Proteinase Inhibitors - pharmacology Stability Sunflowers Trypsin Trypsin inhibitors
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