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Type: Journal article
Title: Photoregulation of α-chymotrypsin activity by spiropyran-based inhibitors in solution and attached to an optical fiber
Other Titles: Photoregulation of alpha-chymotrypsin activity by spiropyran-based inhibitors in solution and attached to an optical fiber
Author: Zhang, X.
Heng, S.
Abell, A.
Citation: Chemistry, 2015; 21(30):10703-10713
Publisher: Wiley
Issue Date: 2015
ISSN: 0947-6539
Statement of
Xiaozhou Zhang, Sabrina Heng, Andrew. D. Abell
Abstract: Here the synthesis and characterization of a new class of spiropyran-based protease inhibitor is reported that can be reversibly photoswitched between an active spiropyran (SP) isomer and a less active merocyanine (MC) isomer upon irradiation with UV and visible light, respectively, both in solution and on a surface of a microstructured optical fiber (MOF). The most potent inhibitor in the series (SP-3 b) has a C-terminal phenylalanyl-based α-ketoester group and inhibits α-chymotrypsin with a Ki of 115 nM. An analogue containing a C-terminal Weinreb amide (SP-2 d) demonstrated excellent stability and photoswitching in solution and was attached to the surface of a MOF. The SP isomer of Weinreb amide 2 d is a competitive reversible inhibitor in solution and also on fiber, while the corresponding MC isomer was significantly less active in both media. The ability of this new class of spiropyran-based protease inhibitor to modulate enzyme activity on a MOF paves the way for sensing applications.
Keywords: enzymes; peptidomimetics; photoswitching, spiropyran; surface chemistry
Rights: © 2015 Wiley-VCH Verlag GmbH &Co. KGaA, Weinheim
RMID: 0030031222
DOI: 10.1002/chem.201501488
Appears in Collections:IPAS publications

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