Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).
Antimony is a metalloid that affects biological functions in humans due to a mechanism still not understood. There is no doubt that the toxicity and physicochemical properties of Sb are strongly related with its chemical state. In this paper, the interaction between Sb(III) and Sb(V) with bovine serum albumin (BSA) was investigated in vitro by fluorescence spectroscopy, and circular dichroism (CD) under simulated physiological conditions. Moreover, the coupling of the separation technique, asymmetric flow field-flow fractionation, with elemental mass spectrometry to understand the interaction of Sb(V) and Sb(III) with the BSA was also used. Our results showed a different behaviour of Sb(III) vs. Sb(V) regarding their effects on the interaction with the BSA. The effects in terms of protein aggregates and conformational changes were higher in the presence of Sb(III) compared to Sb(V) which may explain the differences in toxicity between both Sb species in vivo. Obtained results demonstrated the protective effect of GSH that modifies the degree of interaction between the Sb species with BSA. Interestingly, in our experiments it was possible to detect an interaction between BSA and Sb species, which may be related with the presence of labile complex between the Sb and a protein for the first time.
Instituto de Química, Pontificia Universidad Católica de Valparaíso, Valparaíso, Chile.|Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Marcelo
M
Verdugo
Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Jorge
J
Ruiz Encinar
Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
José Manuel
JM
Costa-Fernández
Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Mario
M
Menendez-Miranda
Department of Physical and Analytical Chemistry, Faculty of Chemistry, University of Oviedo, Oviedo, Spain.
Diego
D
Bouzas-Ramos
Instituto de Química, Pontificia Universidad Católica de Valparaíso, Valparaíso, Chile.
Manuel
M
Bravo
Instituto de Química, Pontificia Universidad Católica de Valparaíso, Valparaíso, Chile.
Waldo
W
Quiroz
D000818:Animals; D000965:Antimony / Q000737:chemistry / Q000633:toxicity*; D002417:Cattle; D002850:Chromatography, Gel; D002942:Circular Dichroism; D031521:Fractionation, Field Flow; D005978:Glutathione / Q000737:chemistry / Q000494:pharmacology; D006801:Humans; D066298:In Vitro Techniques; D066329:Protein Aggregates / Q000187:drug effects*; D011487:Protein Conformation / Q000187:drug effects*; D017433:Protein Structure, Secondary / Q000187:drug effects; D012710:Serum Albumin, Bovine / Q000737:chemistry* / Q000187:drug effects*; D013050:Spectrometry, Fluorescence
D066329:Protein Aggregates; D012710:Serum Albumin, Bovine; D000965:Antimony; D005978:Glutathione