Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies

dc.contributorUniversidade de São Paulo (USP)
dc.contributorUniversidade Estadual de Maringá (UEM)
dc.contributorUniversidade Estadual Paulista (Unesp)
dc.creatorCarvalho, Jose Wilson P.
dc.creatorCarvalho, Francisco Adriano O.
dc.creatorBatista, Tatiana
dc.creatorSantiago, Patricia S. [UNESP]
dc.creatorTabak, Marcel
dc.date2014-12-03T13:11:41Z
dc.date2014-12-03T13:11:41Z
dc.date2014-06-01
dc.date.accessioned2023-09-09T10:15:15Z
dc.date.available2023-09-09T10:15:15Z
dc.identifierhttp://dx.doi.org/10.1016/j.colsurfb.2014.03.021
dc.identifierColloids And Surfaces B-biointerfaces. Amsterdam: Elsevier Science Bv, v. 118, p. 14-24, 2014.
dc.identifier0927-7765
dc.identifierhttp://hdl.handle.net/11449/113414
dc.identifier10.1016/j.colsurfb.2014.03.021
dc.identifierWOS:000337013900003
dc.identifier6705367010662087
dc.identifier0000-0002-6205-9441
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8763013
dc.descriptionGlossoscolex paulistus (HbGp) hemoglobin is an oligomeric protein, displaying a quaternary structure constituted by 144 globin and 36 non-globin chains (named linkers) with a total molecular mass of 3.6 MDa. CTAC effects on the oxy-HbGp thermal stability were investigated, by DLS and SAXS, at pH 5.0, 7.0 and 9.0. DLS data show that the oxy-HbGp-CTAC interactions induce a significant decrease of the protein thermal stability, with the formation of larger aggregates, at pH 5.0 and 7.0. In the acidic pH, oxy-HbGp 0.5 mg/mL, undergoes a partial oligomeric dissociation, on going from 0.2 to 0.6 mmol/L of CTAC, accompanied by a decrease in the D-h values from 27 +/- 1 to 22 +/- 1 nm. It is observed, for the first time, that in the absence and in the presence of CTAC, oxy-HbGp undergoes a partial oligomeric dissociation, with increase of temperature, before denaturation and aggregation at pH values 7.0 and 5.0. SAXS data show that oxy-HbGp undergoes denaturation at 60 degrees C, in the presence of CTAC, pH 5.0. At neutral pH 7.0, the aggregation process starts at 20 degrees C, with increase of R-g and D-max parameters. At both pH values, 5.0 and 7.0, the denaturation and aggregation are accompanied by the sedimentation of the aggregates. At pH 9.0, oxy-HbGp is totally dissociated at 40 degrees C, in the presence of 0.2 mmol/L of CTAC, while in the presence of 0.4 mmol/L of surfactant the aggregation process starts at 20 degrees C, with the full denaturation of protein at higher temperature. Finally, our data show, for the first time, that the oligomeric dissociation is an important step in the thermal denaturation of oxy-HbGp, in the presence of CTAC, independently of both the pH and the protein concentration. (C) 2014 Elsevier B.V. All rights reserved.
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionUniv Sao Paulo, Inst Quim Sao Carlos, Sao Carlos, SP, Brazil
dc.descriptionUniv Estadual Maringa, Maringa, Parana, Brazil
dc.descriptionUniv Estadual Paulista, Registro, SP, Brazil
dc.descriptionUniv Estadual Paulista, Registro, SP, Brazil
dc.descriptionFAPESP: 13/09349-6
dc.descriptionCNPq: 162650/2013-2
dc.format14-24
dc.languageeng
dc.publisherElsevier B.V.
dc.relationColloids and Surfaces B: Biointerfaces
dc.relation3.997
dc.relation1,071
dc.rightsAcesso restrito
dc.sourceWeb of Science
dc.subjectGlossoscolex paulistus
dc.subjectThermal stability
dc.subjectCTAC
dc.subjectDLS
dc.subjectSAXS
dc.titleCetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: Dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies
dc.typeArtigo


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