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Polyethylene glycol crowding effect on hyaluronidase activity monitored by capillary electrophoresis

dc.rights.licenseopenen_US
dc.contributor.authorNASREDDINE, Rouba
dc.contributor.authorORLIC, Lucija
dc.contributor.authorBANNI, Ghassan Al Hamoui Dit
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorFAYAD, Syntia
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorMARCHAL, Axel
dc.contributor.authorPIAZZA, Francesco
dc.contributor.authorLOPIN-BON, Chrystel
dc.contributor.authorHAMACEK, Josef
dc.contributor.authorNEHME, Reine
dc.date.accessioned2021-04-12T13:41:24Z
dc.date.available2021-04-12T13:41:24Z
dc.date.issued2020-05-06
dc.identifier.issn1618-2642en_US
dc.identifier.urioai:crossref.org:10.1007/s00216-020-02659-9
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/26930
dc.description.abstractEnTo mimic the activity of hyaluronidase in natural environment, the hydrolysis of hyaluronic acid (HA) by hyaluronidase was investigated for the first time in the presence of crowding agents using capillary electrophoresis (CE) as a simple and reliable technique for conducting enzymatic assay. Polyethylene glycol (PEG) 6000 was selected as a model crowder and the hyaluronic acid degradation catalyzed by bovine testes hyaluronidase (BTH) was carried out at different PEG concentrations (0%, 10%, and 17%). After optimization of the CE analytical method and enzymatic assay, the degradation products were monitored at different HA concentrations. At 10% of PEG and 0.3 mg mL−1 of HA, the activity of the enzyme was significantly reduced showing inconvenient interactions of PEG with the hyaluronidase blocking the release of hydrolysis products. A similar reduction of hyaluronidase activity was observed at 1 mg mL−1 of HA due to the presumable formation of the BTH-substrate complex. The experimental curves obtained by CE also evidence that the overall kinetics are governed by the hydrolysis of hexasaccharide intermediates. Finally, the effect of PEG on hyaluronidase activity was evaluated in the presence of natural or synthetic inhibitors. Our results show a significant difference of the inhibitors’ affinity toward hyaluronidase in the presence of PEG. Surprisingly, the presence of the crowding agent results in a loss of the inhibition effect of small polycyclic inhibitors, while larger charged inhibitors were less affected. In this work, CE analyses confirm the importance of mimicking the cellular environment for the discovery and development of reliable inhibitors.
dc.language.isoENen_US
dc.sourcecrossref
dc.subject.encapillary electrophoresis
dc.subject.encrowding
dc.subject.enhyaluronidase activity
dc.subject.eninhibitors
dc.subject.enpolysaccharide
dc.title.enPolyethylene glycol crowding effect on hyaluronidase activity monitored by capillary electrophoresis
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s00216-020-02659-9en_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétaleen_US
bordeaux.journalAnalytical and Bioanalytical Chemistryen_US
bordeaux.page4195–4207en_US
bordeaux.volume412en_US
bordeaux.hal.laboratoriesOenologie - EA 4577en_US
bordeaux.issue17en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionINRAEen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcedissemin
hal.exportfalse
workflow.import.sourcedissemin
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