Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb

• Published in: PloS one 2017-02, Vol.12 (2), p.e0170869
• Main Authors: Verdugo, Marcelo, Ruiz Encinar, Jorge, Costa-Fernández, José Manuel, Menendez-Miranda, Mario, Bouzas-Ramos, Diego, Bravo, Manuel, Quiroz, Waldo
• Format: Article
• Language: English
• Subjects: Antimony; Fluorescence spectroscopy; Serum albumin
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0170869

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.