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Nature Research, Scientific Reports, 1(6), 2016

DOI: 10.1038/srep22856

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

Journal article published in 2016 by Magdalena Wysocka, Natalia Gruba, Renata Grzywa, Artur Giełdoń, Remigiusz Bąchor ORCID, Krzysztof Brzozowski, Marcin Sieńczyk, Jenne Dieter, Zbigniew Szewczuk ORCID, Krzysztof Rolka, Adam Lesner
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

AbstractHerein 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.