Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/69595
Title: Exploration of the one-bead one-compound methodology for the design of prolyl oligopeptidase substrates
Author: Comellas, Gemma
Kaczmarska, Zusanna
Tarragó Clua, Maria Teresa
Teixidó Turà, Meritxell
Giralt Lledó, Ernest
Keywords: Cromatografia
Espectrometria de masses
Anàlisi de pèptids
Chromatography
Mass spectrometry
Analysis of peptides
Issue Date: 13-Jul-2009
Publisher: Public Library of Science (PLoS)
Abstract: Here we describe the design, synthesis and evaluation of the first solid-phase substrates for prolyl oligopeptidase (POP), a cytosolic serine peptidase associated with schizophrenia, bipolar affective disorder and related neuropsychiatric disorders. This study seeks to contribute to the future design of a one-bead one-compound (OBOC) peptide library of POP substrates, based on an intramolecular energy transfer substrate. Unexpectedly, the enzymatic evaluation of the substrates attached on solid-phase by means of the HMBA linker were cleaved through the ester bond, thereby suggesting an unknown esterase activity of POP, in addition to its known peptidase activity. By performing multiple activity assays, we have confirmed the esterase activity of this enzyme and its capacity to process the substrates on solid-phase. Finally, we tested a new linker, compatible with both the solid-phase peptide-synthesis used and the enzymatic assay, for application in the future design of an OBOC library.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0006222
It is part of: PLoS One, 2009, vol. 4, num. 7, p. e6222
Related resource: http://dx.doi.org/10.1371/journal.pone.0006222
URI: http://hdl.handle.net/2445/69595
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

Files in This Item:
File Description SizeFormat 
577497.pdf1.03 MBAdobe PDFView/Open


This item is licensed under a Creative Commons License Creative Commons