Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.

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 P1 position and two basic amino acid residues (Lys or/and Arg) in P2' and P3' positions strongly inhibited c...

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Autores principales: Dawid Dębowski, Michał Pikuła, Marta Lubos, Paulina Langa, Piotr Trzonkowski, Adam Lesner, Anna Łęgowska, Krzysztof Rolka
Formato: article
Lenguaje:EN
Publicado: Public Library of Science (PLoS) 2014
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Science
Q
Acceso en línea:https://doaj.org/article/e6fd53a447ef480aa404397e49c46070
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spelling oai:doaj.org-article:e6fd53a447ef480aa404397e49c460702021-11-18T08:31:09ZInhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.1932-620310.1371/journal.pone.0089465https://doaj.org/article/e6fd53a447ef480aa404397e49c460702014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24586798/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Starting 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 P1 position and two basic amino acid residues (Lys or/and Arg) in P2' and P3' 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.Dawid DębowskiMichał PikułaMarta LubosPaulina LangaPiotr TrzonkowskiAdam LesnerAnna ŁęgowskaKrzysztof RolkaPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e89465 (2014)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
Dawid Dębowski
Michał Pikuła
Marta Lubos
Paulina Langa
Piotr Trzonkowski
Adam Lesner
Anna Łęgowska
Krzysztof Rolka
Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.
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 P1 position and two basic amino acid residues (Lys or/and Arg) in P2' and P3' 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.
format article
author Dawid Dębowski
Michał Pikuła
Marta Lubos
Paulina Langa
Piotr Trzonkowski
Adam Lesner
Anna Łęgowska
Krzysztof Rolka
author_facet Dawid Dębowski
Michał Pikuła
Marta Lubos
Paulina Langa
Piotr Trzonkowski
Adam Lesner
Anna Łęgowska
Krzysztof Rolka
author_sort Dawid Dębowski
title 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_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_sort inhibition of human and yeast 20s proteasome by analogues of trypsin inhibitor sfti-1.
publisher Public Library of Science (PLoS)
publishDate 2014
url https://doaj.org/article/e6fd53a447ef480aa404397e49c46070
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AT adamlesner inhibitionofhumanandyeast20sproteasomebyanaloguesoftrypsininhibitorsfti1
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