Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V)

Abstract

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.

Preparation of 68Ga‐Mg‐Ca‐phytate colloid and its evaluation as a liver imaging agent

“…After intravenous injection of 67 Ga‐citrate, 21% of the radioactivity was shown to be associated with the erythrocytes, and 79% was bound to plasma proteins in which 88% was 67 Ga‐transferrin . Albumin is the prevalent protein in the remaining plasma pool, and it can strongly bind metal complexes via the ligand, or with metal ions directly …”

“…42 Albumin is the prevalent protein in the remaining plasma pool, and it can strongly bind metal complexes via the ligand, 27 or with metal ions directly. 43,44 A frequent characteristic of radiogallium scans in patients with cancer or infection is low salivary glands uptake. 45 Salivary uptake of radioactive-transferrin was not seen in early or delayed images of normal animals ( 45 Ti, 18 F), and of rodents with cancer ( 89 Zr, 45 Ti) or a focal infection ( 99m Tc).…”

Ribosylation induced structural changes in Bovine Serum Albumin: understanding high dietary sugar induced protein aggregation and amyloid formation

“…One of the major cellular complicacies arising out of consistent persistence of reducing sugars is posed by non-enzymatic glycation of proteins leading to their subsequent aggregation. Protein aggregation is implicated in many detrimental conditions ranging from neurodegenerative diseases to degeneration of therapeutically important proteins [ 1 , 2 ]. Despite protein folding and protein aggregation being distinct processes, both intrinsic and extrinsic factors govern whether a folding pathway will lead to a native structure or to misfolded aggregate [ 3 ].…”

“…Additionally, the methodology used universally to glycate proteins involves incubation of the protein with the respective sugars at 37 °C. Sustained incubation at such elevated temperatures is known to cause structural alterations in the protein [ 2 , 26 ] including formation of aggregates. However, most of the studies have not systematically accounted for the changes which occur in the control non glycated protein incubated under similar conditions.…”

Risk of Cancer for Workers Exposed to Antimony Compounds: A Systematic Review

“…In its positive pentavalent form, it may be a part of antimony pentafluoride or antimony pentachloride [1]. It is thought that the trivalent form is more active in vivo [2]. Prevalent antimony compounds are listed in Table 1.…”