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

ABSTRACT: 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.

SUBMITTER: Wysocka M

PROVIDER: S-EPMC4783772 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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

Wysocka Magdalena M Gruba Natalia N Grzywa Renata R Giełdoń Artur A Bąchor Remigiusz R Brzozowski Krzysztof K Sieńczyk Marcin M Dieter Jenne J Szewczuk Zbigniew Z Rolka Krzysztof K Lesner Adam A

Scientific reports 20160309

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 ...[more]

PMID: 26955973

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