Journal
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
Volume 250, Issue -, Pages -Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.saa.2020.119350
Keywords
Gemini surfactant; BSA; Interaction; Fluorescence quenching; Molecular modeling
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The interaction between pyridinium based gemini surfactants and bovine serum albumin was studied using a combination of experimental and computational techniques, revealing the impact of the surfactants on the protein structure and secondary structure.
To study the interaction of the series of pyridinium based gemini surfactants (GS) (referred to as m-Py-m, m = 14, 16); 4,4'-(propane-1,3-diyl)bis(1-(2-(tetradecyloxy)-2-oxoethyl) dipyridinium chloride (14-Py-14), and 4,4'-(propane-1,3-diyl) bis(1-(2-(hexadecyloxy)-2-oxoethyl)dipyridinium chloride (16-Py-16) with bovine serum albumin (BSA), various physicochemical and spectroscopic tools such as tensiometry, steady-state fluorescence, synchronous fluorescence, pyrene fluorescence, UV-visible, far-UV circular dichroism (CD) were utilized at physiological pH (7.4) and 298 K in combination with computational molecular modeling analysis. The tensiometric results show significant modifications in interfacial and thermodynamic parameters for m-Py-m GS upon BSA combination, deciphering the gemini surfactant-BSA interaction. Steady-state fluorescence analysis evaluates the structural alterations of BSA with the addition of m-Py-m GS. The plots of Stern-Volmer, modified Stern-Volmer, and thermodynamic parameters were used to determine the binding type of m-Py-m GS to BSA. The synchronous fluorescence spectra state a mild effect of gemini surfactants on the emission intensity of tyrosine (Tyr) residues, on the other hand, tryptophan (Trp) residues showed a significant effect. Post addition of GS, the plot of pyrene fluorescence reveals the mild micropolarity fluctuations via the probe (pyrene) molecules encapsulated in BSA. UV-visible experiments support the complex formation between the BSA and m-Py-m GS. Far UV CD measurements revealed the modifications in the secondary structure of protein produced by m-Py-m GS. Furthermore, we also used the computational molecular modeling for attaining deep insight into BSA and m-Py-m GS binding and the results are supported with our experimental results. (C) 2020 Elsevier B.V. All rights reserved.
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