期刊
ANALYTICAL BIOCHEMISTRY
卷 508, 期 -, 页码 38-45出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ab.2015.08.019
关键词
20S Eukaryotic proteasome; Internally quenched peptides; Fluorescence
资金
- Polish Ministry of Science and Higher Education (Iuventus Plus) [0624/IP32011/7]
- Polish National Science Center [UMO-2011/01/D/ST5/02778]
This article describes the synthesis, using combinatorial chemistry, of internally quenched substrates of the trypsin-like subunit of human 20S proteasome. Such substrates were optimized in both the nonprime and prime regions of the peptide chain. Two were selected as the most susceptible for proteasomal proteolysis with excellent kinetic parameters: (i) ABZ-Val-Val-Ser-Arg-Ser-Leu-Gly-Tyr(3-NO2)-NH2 (k(cat)/ K-M = 934,000 M-1 s(-1)) and (ii) ABZ-Val-Val-Ser-GNF-Ala-Met-Gly-Tyr(3-NO2)-NH2 (k(cat)/ K-M = 1,980,000 M-1 s(-1)). Both compounds were efficiently hydrolyzed by the 20S proteasome at picomolar concentrations, demonstrating significant selectivity over other proteasome entities. (C) 2015 Elsevier Inc. All rights reserved.
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