Novel internally quenched substrate of the trypsin-like subunit of 20S eukaryotic proteasome.
Anal Biochem
; 508: 38-45, 2016 09 01.
Article
en En
| MEDLINE
| ID: mdl-26314791
ABSTRACT
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 (kcat/KM = 934,000 M(-1) s(-1)) and (ii) ABZ-Val-Val-Ser-GNF-Ala-Met-Gly-Tyr(3-NO2)-NH2 (kcat/KM = 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.
Palabras clave
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Péptidos
/
Tripsina
/
Complejo de la Endopetidasa Proteasomal
Límite:
Humans
Idioma:
En
Año:
2016
Tipo del documento:
Article