Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1

Starting from the primary structure of sunflower trypsin inhibitor SFTI-1, we designed novel non-covalent inhibitors of human and yeast 20S proteasomes. Peptides with Arg residue in P(1) position and two basic amino acid residues (Lys or/and Arg) in P(2)′ and P(3)′ positions strongly inhibited chymo...

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Detalles Bibliográficos
Autores principales: Dębowski, Dawid, Pikuła, Michał, Lubos, Marta, Langa, Paulina, Trzonkowski, Piotr, Lesner, Adam, Łęgowska, Anna, Rolka, Krzysztof
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2014
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3934894/
https://www.ncbi.nlm.nih.gov/pubmed/24586798
http://dx.doi.org/10.1371/journal.pone.0089465
Descripción
Sumario:Starting from the primary structure of sunflower trypsin inhibitor SFTI-1, we designed novel non-covalent inhibitors of human and yeast 20S proteasomes. Peptides with Arg residue in P(1) position and two basic amino acid residues (Lys or/and Arg) in P(2)′ and P(3)′ positions strongly inhibited chymotrypsin-like and caspase-like activities, while trypsin-like activity was poorly modified. We found that some SFTI-1 analogues up-regulated exclusively the chymotrypsin-like activity of latent yeast 20S proteasome.

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