PEGylated substrates of NSP4 protease: A tool to study protease specificity

Herein we present the synthesis of a novel type of peptidomimetics composed of repeating diaminopropionic acid residues modified with structurally diverse heterobifunctional polyethylene glycol chains (abbreviated as DAPEG). Based on the developed compounds, a library of fluorogenic substrates was s...

Descripción completa

Detalles Bibliográficos
Autores principales: Wysocka, Magdalena, Gruba, Natalia, Grzywa, Renata, Giełdoń, Artur, Bąchor, Remigiusz, Brzozowski, Krzysztof, Sieńczyk, Marcin, Dieter, Jenne, Szewczuk, Zbigniew, Rolka, Krzysztof, Lesner, Adam
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2016
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4783772/
https://www.ncbi.nlm.nih.gov/pubmed/26955973
http://dx.doi.org/10.1038/srep22856
_version_ 1782420162164555776
author Wysocka, Magdalena
Gruba, Natalia
Grzywa, Renata
Giełdoń, Artur
Bąchor, Remigiusz
Brzozowski, Krzysztof
Sieńczyk, Marcin
Dieter, Jenne
Szewczuk, Zbigniew
Rolka, Krzysztof
Lesner, Adam
author_facet Wysocka, Magdalena
Gruba, Natalia
Grzywa, Renata
Giełdoń, Artur
Bąchor, Remigiusz
Brzozowski, Krzysztof
Sieńczyk, Marcin
Dieter, Jenne
Szewczuk, Zbigniew
Rolka, Krzysztof
Lesner, Adam
author_sort Wysocka, Magdalena
collection PubMed
description Herein we present the synthesis of a novel type of peptidomimetics composed of repeating diaminopropionic acid residues modified with structurally diverse heterobifunctional polyethylene glycol chains (abbreviated as DAPEG). Based on the developed compounds, a library of fluorogenic substrates was synthesized. Further library deconvolution towards human neutrophil serine protease 4 (NSP4) yielded highly sensitive and selective internally quenched peptidomimetic substrates. In silico analysis of the obtained peptidomimetics revealed the presence of an interaction network with distant subsites located on the enzyme surface.
format Online
Article
Text
id pubmed-4783772
institution National Center for Biotechnology Information
language English
publishDate 2016
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-47837722016-03-11 PEGylated substrates of NSP4 protease: A tool to study protease specificity Wysocka, Magdalena Gruba, Natalia Grzywa, Renata Giełdoń, Artur Bąchor, Remigiusz Brzozowski, Krzysztof Sieńczyk, Marcin Dieter, Jenne Szewczuk, Zbigniew Rolka, Krzysztof Lesner, Adam Sci Rep Article Herein we present the synthesis of a novel type of peptidomimetics composed of repeating diaminopropionic acid residues modified with structurally diverse heterobifunctional polyethylene glycol chains (abbreviated as DAPEG). Based on the developed compounds, a library of fluorogenic substrates was synthesized. Further library deconvolution towards human neutrophil serine protease 4 (NSP4) yielded highly sensitive and selective internally quenched peptidomimetic substrates. In silico analysis of the obtained peptidomimetics revealed the presence of an interaction network with distant subsites located on the enzyme surface. Nature Publishing Group 2016-03-09 /pmc/articles/PMC4783772/ /pubmed/26955973 http://dx.doi.org/10.1038/srep22856 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Wysocka, Magdalena
Gruba, Natalia
Grzywa, Renata
Giełdoń, Artur
Bąchor, Remigiusz
Brzozowski, Krzysztof
Sieńczyk, Marcin
Dieter, Jenne
Szewczuk, Zbigniew
Rolka, Krzysztof
Lesner, Adam
PEGylated substrates of NSP4 protease: A tool to study protease specificity
title PEGylated substrates of NSP4 protease: A tool to study protease specificity
title_full PEGylated substrates of NSP4 protease: A tool to study protease specificity
title_fullStr PEGylated substrates of NSP4 protease: A tool to study protease specificity
title_full_unstemmed PEGylated substrates of NSP4 protease: A tool to study protease specificity
title_short PEGylated substrates of NSP4 protease: A tool to study protease specificity
title_sort pegylated substrates of nsp4 protease: a tool to study protease specificity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4783772/
https://www.ncbi.nlm.nih.gov/pubmed/26955973
http://dx.doi.org/10.1038/srep22856
work_keys_str_mv AT wysockamagdalena pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT grubanatalia pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT grzywarenata pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT giełdonartur pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT bachorremigiusz pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT brzozowskikrzysztof pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT sienczykmarcin pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT dieterjenne pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT szewczukzbigniew pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT rolkakrzysztof pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity
AT lesneradam pegylatedsubstratesofnsp4proteaseatooltostudyproteasespecificity

Ejemplares similares