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Spectral characterization of the binding and conformational changes of bovine serum albumin upon interaction with an anti-fungal drug, methylparaben.


Spectrochim Acta A Mol Biomol Spectrosc. 2013 Jan 2;105C:418-423


Authors: Naik KM, Nandibewoor ST


Abstract

The binding of methylparaben with bovine serum albumin (BSA) was investigated by spectroscopic methods viz., fluorescence, FT-IR and UV-vis absorption techniques under physiological conditions i.e., pH 7.4. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of bovine serum albumin by methylparaben shows a dynamic quenching. The binding sites number n and binding constants, K were obtained at various temperatures. The distance, r between methylparaben and BSA was evaluated according to the theory of Förster energy transfer. The result of FT-IR spectra and UV-vis absorption spectra showed that the conformation of bovine serum albumin has been changed in the presence of methylparaben. The thermodynamic parameters, enthalpy change (ΔH(0)) and entropy change (ΔS(0)) were calculated according to van't Hoff equation, which indicated that the hydrophobic interaction was the predominant intermolecular force stabilizing the complex. The effect of common ions and site probes were also carried on the binding of methylparaben to BSA.

PMID: 23334503 [PubMed - as supplied by publisher]