2026-04-17T07:44:13Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/695952025-12-04T21:45:36Zcom_2072_1057col_2072_478917col_2072_478933

00925njm 22002777a 4500 dc Comellas, Gemma author Kaczmarska, Zuzanna author Tarragó Clua, Maria Teresa author Teixidó Turà, Meritxell author Giralt Lledó, Ernest author 2016-02-18T12:40:33Z 2016-02-18T12:40:33Z 2009-07-13 2016-02-18T12:40:33Z 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. Cromatografia Espectrometria de masses Anàlisi de pèptids Chromatography Mass spectrometry Analysis of peptides Exploration of the one-bead one-compound methodology for the design of prolyl oligopeptidase substrates