Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorCarvalho, José Wilson P.
dc.creatorAlves, Fernanda Rosa
dc.creatorBatista, Tatiana
dc.creatorCarvalho, Francisco Adriano O.
dc.creatorSantiago, Patrícia S.
dc.creatorTabak, Marcel
dc.date2014-05-27T11:30:52Z
dc.date2016-10-25T18:55:03Z
dc.date2014-05-27T11:30:52Z
dc.date2016-10-25T18:55:03Z
dc.date2013-11-01
dc.date.accessioned2017-04-06T02:42:08Z
dc.date.available2017-04-06T02:42:08Z
dc.identifierColloids and Surfaces B: Biointerfaces, v. 111, p. 561-570.
dc.identifier0927-7765
dc.identifier1873-4367
dc.identifierhttp://hdl.handle.net/11449/76888
dc.identifierhttp://acervodigital.unesp.br/handle/11449/76888
dc.identifier10.1016/j.colsurfb.2013.06.050
dc.identifierWOS:000324897900074
dc.identifier2-s2.0-84880992766
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2013.06.050
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/897569
dc.descriptionGlossoscolex paulistus (HbGp) hemoglobin is an oligomeric protein, presenting a quaternary structure constituted by 144 globin and 36 non-globin chains (named linkers) with a total molecular mass of 3.6MDa. SDS effects on the oxy-HbGp thermal stability were studied, by DLS and SAXS, at pH 5.0, 7.0 and 9.0. DLS and SAXS data show that the SDS-oxy-HbGp interactions induce a significant decrease of the protein thermal stability, with the formation of larger aggregates, at pH 5.0. At pH 7.0, oxy-HbGp undergoes complete oligomeric dissociation, with increase of temperature, in the presence of SDS. Besides, oxy-HbGp 3.0mg/mL, pH 7.0, in the presence of SDS, has the oligomeric dissociation process reduced as compared to 0.5mg/mL of protein. At pH 9.0, oxy-HbGp starts to dissociate at 20°C, and the protein is totally dissociated at 50°C. The thermal dissociation kinetic data show that oxy-HbGp oligomeric dissociation at pH 7.0, in the presence of SDS, is strongly dependent on the protein concentration. At 0.5mg/mL of protein, the oligomeric dissociation is complete and fast at 40 and 42°C, with kinetic constants of (2.1±0.2)×10-4 and (5.5±0.4)×10-4s-1, respectively, at 0.6mmol/L SDS. However, at 3.0mg/mL, the oligomeric dissociation process starts at 46°C, and only partial dissociation, accompanied by aggregates formation is observed. Moreover, our data show, for the first time, that, for 3.0mg/mL of protein, the oligomeric dissociation, denaturation and aggregation phenomena occur simultaneously, in the presence of SDS. Our present results on the surfactant-HbGp interactions and the protein thermal unfolding process correspond to a step forward in the understanding of SDS effects. © 2013 Elsevier B.V.
dc.languageeng
dc.relationColloids and Surfaces B: Biointerfaces
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectDLS
dc.subjectGlossoscolex paulistus
dc.subjectOligomeric dissociation
dc.subjectSAXS
dc.subjectSDS
dc.subjectThermal stability
dc.subjectAggregation phenomena
dc.subjectProtein concentrations
dc.subjectProtein thermal stability
dc.subjectSmall angle X-ray scattering
dc.subjectAggregates
dc.subjectDissociation
dc.subjectDynamic light scattering
dc.subjectHemoglobin
dc.subjectOligomers
dc.subjectProteins
dc.subjectThermodynamic stability
dc.subjectSodium dodecyl sulfate
dc.subjectdodecyl sulfate sodium
dc.subjectGlossoscolex paulistus hemoglobin
dc.subjecthemoglobin
dc.subjectoligomer
dc.subjectunclassified drug
dc.subjectconcentration (parameters)
dc.subjectcontrolled study
dc.subjectdissociation
dc.subjectdynamic light scattering
dc.subjecthigh temperature procedures
dc.subjectkinetics
dc.subjectlight scattering
dc.subjectmolecular weight
dc.subjectpH
dc.subjectpriority journal
dc.subjectprotein aggregation
dc.subjectprotein denaturation
dc.subjectprotein interaction
dc.subjectprotein stability
dc.subjectprotein unfolding
dc.subjectthermostability
dc.subjectX ray crystallography
dc.titleSodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies
dc.typeOtro


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