Abstract
The interaction of bisphenol-S (BPS) with serum albumins using steady-state, synchronous, time-resolved, and circular dichroism spectroscopies has been investigated. The binding interactions have also been investigated in the case of bisphenol A (BPA). The fluorescence quenching pathways are different for both of these endocrine disrupting compounds. Steady-state and time-resolved studies reveal static quenching at lower concentrations of BPS and dynamic quenching at higher concentrations. CD results also maintained the concentration dependent variation with a complete distortion of α-helices at 10(-5) M BPS. Besides this, addition of sodium dodecyl sulfate (SDS) results in the further unfolding of protein in the case of BPS, whereas time-resolved studies indicated refolding for BPA denatured human serum albumin (HSA). The entire study indicates an irreversible binding of BPS with HSA. Hence, these results reveal the possible involvement of BPS in the physiological pathway raising a health threat as already their presences in body fluids are known.
Published Version
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