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Autor
Ball, Kathryn 1 Gil-Mir, Maria 1 Hernychova, Lenka 1 Huart, Anne-Sophie 1 Hupp, Ted 1 Jurczak, Przemyslaw 1 Kalathiya, Umesh 1 Krejci, Adam 1 Krejcir, Radovan 1 Lickiss, Fiona 1 Lisowska, Małgorzata 1 Muller, Petr 1 Rodziewicz-Motowidło, Sylwia 1 Trybala, Zuzanna 1 Vojtesek, Borivoj 1 Way, Luke 1 Zhukow, Igor 1
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Autor
Ball, Kathryn 1 Gil-Mir, Maria 1 Hernychova, Lenka 1 Huart, Anne-Sophie 1 Hupp, Ted 1 Jurczak, Przemyslaw 1 Kalathiya, Umesh 1 Krejci, Adam 1 Krejcir, Radovan 1 Lickiss, Fiona 1 Lisowska, Małgorzata 1 Muller, Petr 1 Rodziewicz-Motowidło, Sylwia 1 Trybala, Zuzanna 1 Vojtesek, Borivoj 1 Way, Luke 1 Zhukow, Igor 1
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Free Medical Journals od 2010
PubMed Central od 2010
Europe PubMed Central od 2010
Open Access Digital Library od 2010-01-01
Open Access Digital Library od 2010-01-01
ROAD: Directory of Open Access Scholarly Resources od 2010
PubMed
36532480
DOI
10.3389/fmicb.2022.875556
Knihovny.cz E-zdroje
Defining dynamic protein-protein interactions in the ubiquitin conjugation reaction is a challenging research area. Generating peptide aptamers that target components such as ubiquitin itself, E1, E2, or E3 could provide tools to dissect novel features of the enzymatic cascade. Next-generation deep sequencing platforms were used to identify peptide sequences isolated from phage-peptide libraries screened against Ubiquitin and its ortholog NEDD8. In over three rounds of selection under differing wash criteria, over 13,000 peptides were acquired targeting ubiquitin, while over 10,000 peptides were selected against NEDD8. The overlap in peptides against these two proteins was less than 5% suggesting a high degree in specificity of Ubiquitin or NEDD8 toward linear peptide motifs. Two of these ubiquitin-binding peptides were identified that inhibit both E3 ubiquitin ligases MDM2 and CHIP. NMR analysis highlighted distinct modes of binding of the two different peptide aptamers. These data highlight the utility of using next-generation sequencing of combinatorial phage-peptide libraries to isolate peptide aptamers toward a protein target that can be used as a chemical tool in a complex multi-enzyme reaction.
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Po ukončení testovacího provozu bude odkaz přesměrován adresu produkční verze portálu Medvik.