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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
Carvalho, Jose Wilson P. [1] ; Alves, Fernanda Rosa [1] ; Batista, Tatiana [1, 2] ; Carvalho, Francisco Adriano O. [1] ; Santiago, Patricia S. [1, 3] ; Tabak, Marcel [1]
Total Authors: 6
Affiliation:
[1] Univ Sao Paulo, Inst Quim Sao Carlos, Sao Carlos, SP - Brazil
[2] Univ Estadual Maringa, Maringa, Parana - Brazil
[3] Univ Estadual Paulista, Registro, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: COLLOIDS AND SURFACES B-BIOINTERFACES; v. 111, p. 561-570, NOV 1 2013.
Web of Science Citations: 7
Abstract

Glossoscolex 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 3.6 MDa. 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 SOS. Besides, oxy-HbGp 3.0 mg/mL, pH 7.0, in the presence of SDS, has the oligomeric dissociation process reduced as compared to 0.5 mg/mL of protein. At pH 9.0, oxy-HbGp starts to dissociate at 20 degrees C, and the protein is totally dissociated at 50 degrees 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 0.5 mg/mL of protein, the oligomeric dissociation is complete and fast at 40 and 42 degrees C, with kinetic constants of (2.1 +/- 0.2) x 10(-4) and (5.5 +/- 0.4) x 10(-4)s(-1), respectively, at 0.6 mmol/L SOS. However, at 3.0 mg/mL, the oligomeric dissociation process starts at 46 degrees C, and only partial dissociation, accompanied by aggregates formation is observed. Moreover, our data show, for the first time, that, for 3.0 mg/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. (C) 2013 Elsevier B.V. All rights reserved. (AU)

FAPESP's process: 09/17261-6 - Oligomeric stability studies of giant extracellular hemoglobin of Glossoscolex paulistus (HbGp) in the presence of chaotropic agents, surfactants and characterization of its subunits.
Grantee:Francisco Adriano de Oliveira Carvalho
Support Opportunities: Scholarships in Brazil - Doctorate
FAPESP's process: 11/09863-6 - Analysis of giant extracellular hemoglobin from Glossoscolex paulistus (HbGp) and ionic surfactants interaction by isothermal titration calorimetry
Grantee:Fernanda Rosa Alves
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 10/09719-0 - Effects of surfactants, iron oxidation state and medium pH upon the thermal stability of giant extracellular hemoglobin of Glossoscolex paulistus in its native oligomeric form and for trimeric ABC and monomeric d globin subunits
Grantee:José Wilson Pires Carvalho
Support Opportunities: Scholarships in Brazil - Doctorate