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Diarylethene‐Based Photoswitchable Inhibitors of Serine Proteases

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.

Angewandte Chemie (International ed.), 2021-09, Vol.60 (40), p.21789-21794 [Periódico revisado por pares]

Germany: Wiley Subscription Services, Inc

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Título:
Diarylethene‐Based Photoswitchable Inhibitors of Serine Proteases
Autor: 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.
Assuntos: 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
É parte de: Angewandte Chemie (International ed.), 2021-09, Vol.60 (40), p.21789-21794
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Descrição: 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 nanomolar range, whose activity could be modulated over 20‐fold by irradiation. The inhibitory potency as well as resistance to proteolytic degradation were systematically studied on a series of 17 SFTI‐1 analogues. The hydrogen bond network that stabilizes the structure of inhibitors and possibly the enzyme–inhibitor binding dynamics were affected by isomerization of the photoswitch. The feasibility of manipulating enzyme activity in time and space was demonstrated by controlled digestion of gelatin‐based hydrogel and an antimicrobial peptide BP100‐RW. Finally, our design principles of diarylethene photoswitches are shown to apply also for the development of other serine protease inhibitors. Bicyclic diarylethene‐containing analogues of the sunflower trypsin inhibitor‐1 (SFTI‐1) can modulate activity of serine proteases in the nanomolar–micromolar range in highly efficient photocontrollable manner.
Editor: Germany: Wiley Subscription Services, Inc
Idioma: Inglês

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Diarylethene‐Based Photoswitchable Inhibitors of Serine Proteases

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.

Germany: Wiley Subscription Services, Inc

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