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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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
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author Dębowski, Dawid
Pikuła, Michał
Lubos, Marta
Langa, Paulina
Trzonkowski, Piotr
Lesner, Adam
Łęgowska, Anna
Rolka, Krzysztof
author_facet Dębowski, Dawid
Pikuła, Michał
Lubos, Marta
Langa, Paulina
Trzonkowski, Piotr
Lesner, Adam
Łęgowska, Anna
Rolka, Krzysztof
author_sort Dębowski, Dawid
collection PubMed
description 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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spelling pubmed-39348942014-03-04 Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1 Dębowski, Dawid Pikuła, Michał Lubos, Marta Langa, Paulina Trzonkowski, Piotr Lesner, Adam Łęgowska, Anna Rolka, Krzysztof PLoS One Research Article 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. Public Library of Science 2014-02-25 /pmc/articles/PMC3934894/ /pubmed/24586798 http://dx.doi.org/10.1371/journal.pone.0089465 Text en © 2014 Dębowski et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Dębowski, Dawid
Pikuła, Michał
Lubos, Marta
Langa, Paulina
Trzonkowski, Piotr
Lesner, Adam
Łęgowska, Anna
Rolka, Krzysztof
Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title_full Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title_fullStr Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title_full_unstemmed Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title_short Inhibition of Human and Yeast 20S Proteasome by Analogues of Trypsin Inhibitor SFTI-1
title_sort inhibition of human and yeast 20s proteasome by analogues of trypsin inhibitor sfti-1
topic Research Article
url 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
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