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PEGylated substrates of NSP4 protease: A tool to study protease specificity.
Sci. Rep. 6:22856 (2016)
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.
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1.589
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7
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Combinatorial Libraries; Neutrophil Elastase; Peptide; Design; Analogs; Impact; Papain; Probes
Language
english
Publication Year
2016
HGF-reported in Year
2016
ISSN (print) / ISBN
2045-2322
e-ISSN
2045-2322
Journal
Scientific Reports
Quellenangaben
Volume: 6,
Article Number: 22856
Publisher
Nature Publishing Group
Publishing Place
London
Reviewing status
Peer reviewed
Institute(s)
Institute of Lung Health and Immunity (LHI)
POF-Topic(s)
30202 - Environmental Health
Research field(s)
Lung Research
PSP Element(s)
G-501600-005
PubMed ID
26955973
WOS ID
WOS:000371605900002
Scopus ID
84960349715
Erfassungsdatum
2016-03-14