PuSH - Publikationsserver des Helmholtz Zentrums München

Wysocka, M.* ; Gruba, N.* ; Grzywa, R.* ; Giełdoń, A.* ; Bąchor, R.* ; Brzozowski, K.* ; Sienczyk, M.* ; Jenne, D. ; Szewczuk, Z.* ; Rolka, K.* ; Lesner, A.*

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

Sci. Rep. 6:22856 (2016)
Verlagsversion DOI PMC
Open Access Gold
Creative Commons Lizenzvertrag
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.
Altmetric
Weitere Metriken?
Zusatzinfos bearbeiten [➜Einloggen]
Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Combinatorial Libraries; Neutrophil Elastase; Peptide; Design; Analogs; Impact; Papain; Probes
ISSN (print) / ISBN 2045-2322
e-ISSN 2045-2322
Zeitschrift Scientific Reports
Quellenangaben Band: 6, Heft: , Seiten: , Artikelnummer: 22856 Supplement: ,
Verlag Nature Publishing Group
Verlagsort London
Begutachtungsstatus