Počet záznamů: 1
Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures
- 1. 0424813 - BC-A 2015 RIV US eng J - Článek v odborném periodiku
Semashko, T. A. - Vorotnikova, E. A. - Sharikova, V. F. - Vinokurov, Konstantin - Smirnova, Y. A. - Dunaevsky, Y. E. - Belozersky, M. A. - Oppert, B. - Elpidina, E. N. - Filippova, I. Y.
Selective chromogenic and fluorogenic peptide substrates for the assay of cysteine peptidases in complex mixtures.
Analytical Biochemistry. Roč. 449, č. 1 (2014), s. 179-187. ISSN 0003-2697
Grant ostatní:Russian Foundation for Basic Research(RU) 12-04-01562-a; Russian Foundation for Basic Research(RU) 12-03-01057-a; ISTC(RU) 3455
Institucionální podpora: RVO:60077344
Klíčová slova: cysteine peptidases * substrates of peptidases * selective peptide substrates
Kód oboru RIV: CE - Biochemie
Impakt faktor: 2.219, rok: 2014
This study describes the design, synthesis, and use of selective peptide substrates for cysteine peptidases of the C1 papain family, important in many biological processes. The structure of the newly synthesized substrates is Glp-Xaa-Ala-Y (where Glp = pyroglutamyl; Xaa = Phe or Val; and Y = pNA [p -nitroanilide], AMC [4-amino-7-methylcoumaride], or AFC [4-amino-7- trifluoromethyl-coumaride]). Substrates were synthesized enzymatically to guarantee selectivity of the reaction and optical purity of the target compounds, simplifying the scheme of synthesis and isolation of products. The hydrolysis of the synthesized substrates was evaluated by C1 cysteine peptidases from different organisms and with different functions, including plant enzymes papain, bromelain, ficin, and mammalian lysosomal cathepsins B and L. The new substrates were selective for C1 cysteine peptidases and were not hydrolyzed by serine, aspartic, or metallo peptidases. We demonstrated an application of the selectivity of the synthesized substrates.
Trvalý link: http://hdl.handle.net/11104/0233151