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Design of a Selective Substrate and Activity Based Probe for Human Neutrophil Serine Protease 4

By Paulina Kasperkiewicz (769754), Marcin Poreba (182908), Scott J. Snipas (769755), S. Jack Lin (252513), Daniel Kirchhofer (769756), Guy S. Salvesen (182933) and Marcin Drag (182942)


<div><p>Human neutrophil serine protease 4 (NSP4), also known as PRSS57, is a recently discovered fourth member of the neutrophil serine proteases family. Although its biological function is not precisely defined, it is suggested to regulate neutrophil response and innate immune reactions. To create optimal substrates and visualization probes for NSP4 that distinguish it from other NSPs we have employed a Hybrid Combinatorial Substrate Library approach that utilizes natural and unnatural amino acids to explore protease subsite preferences. Library results were validated by synthesizing individual substrates, leading to the identification of an optimal substrate peptide. This substrate was converted to a covalent diphenyl phosphonate probe with an embedded biotin tag. This probe demonstrated high inhibitory activity and stringent specificity and may be suitable for visualizing NSP4 in the background of other NSPs.</p></div

Topics: Biological Sciences, visualizing NSP 4, NSP 4, substrate peptide, protease subsite preferences, prss, visualization probes, library results, Selective Substrate, Human Neutrophil Serine Protease 4 Human neutrophil serine protease 4, Hybrid Combinatorial Substrate Library approach, neutrophil serine proteases family, neutrophil response, covalent diphenyl phosphonate probe, biotin tag
Year: 2015
DOI identifier: 10.1371/journal.pone.0132818
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Provided by: FigShare
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