Please use this identifier to cite or link to this item: http://rdcb.cbg.ipn.mx/handle/20.500.12273/132
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dc.rights.licensehttp://creativecommons.org/about/cc0/es_MX
dc.creatorCLAUDIA GUADALUPE BENITEZ CARDOZA-
dc.date.accessioned2018-07-11T03:55:09Z-
dc.date.available2018-07-11T03:55:09Z-
dc.date.issued2014-04-24-
dc.identifier.urihttp://rdcb.cbg.ipn.mx/handle/20.500.12273/132-
dc.description.abstractEhCP-B9, a cysteine protease (CP) involved in Entamoeba histolytica virulence, is a potential target for disease diagnosis and drug design. After purification from inclusion bodies produced in Escherichia coli, the recombinant EhCP-B9 precursor (ppEhCP-B9) can be refolded using detergents as artificial chaperones. However, the conformational changes that occur during ppEhCP-B9 refolding remain unknown. Here, we comprehensively describe conformational changes of ppEhCP-B9 that are induced by various chemical detergents acting as chaperones, including non-ionic, zwitterionic, cationic and anionic surfactants.Wemonitored the effect of detergent concentration and incubation time on the secondary and tertiary structures of ppEhCP-B9 using fluorescence and circular dichroism (CD) spectroscopy. In the presence of non-ionic and zwitterionic detergents, ppEhCP-B9 adopted a β- enriched structure (ppEhCP-B9β1) without proteolytic activity at all detergent concentrations and incubation times evaluated. ppEhCP-B9 also exhibits a β-rich structure in lowconcentrations of ionic detergents, but at concentrations above the critical micelle concentration (CMC), the protein acquires an α + β structure, similar to that of papain but without proteolytic activity (ppEhCP-B9α + β1). Interestingly, only within a narrow range of experimental conditions in which SDS concentrations were below the CMC, ppEhCP-B9 refolded into a β-sheet rich structure (ppEhCP-B9β2) that slowly transforms into a different type of α + β conformation that exhibited proteolytic activity (ppEhCP-B9α + β2) suggesting that enzymatic activity is gained as slow transformation occurs.es_MX
dc.language.isoenges_MX
dc.rightsinfo:eu-repo/semantics/openAccesses_MX
dc.sourceBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics.Vol. 1844 (7). Jul 2014-
dc.titleConformational changes induced by detergents during the refolding of chemically denatured cysteine protease ppEhCP-B9 from Entamoeba histolyticaes_MX
dc.typeinfo:eu-repo/semantics/articlees_MX
dc.creator.idinfo:eu-repo/dai/mx/cvu/25026-
dc.subject.ctiinfo:eu-repo/classification/cti/2es_MX
dc.subject.keywordsCysteine protease; Entamoeba histolytica; SDS; Protein folding; Chemical denaturationes_MX
dc.type.versioninfo:eu-repo/semantics/publishedVersiones_MX
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