Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study

Akram, M. and Anwar, S. and Bhat, I.A. and Kabir-Ud-, Din (2017) Multifaceted Analysis of the Noncovalent Interactions of Myoglobin with Finely Tuned Gemini Surfactants: A Comparative Study. Industrial and Engineering Chemistry Research, 56 (46). pp. 13663-13676. ISSN 8885885

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Official URL: http://pubs.acs.org/doi/10.1021/acs.iecr.7b01583

Abstract

This work unveils the noncovalent interactions of a novel series of finely tuned gemini surfactants (Cm-E2O-Cm, m = 12, 14, and 16) with myoglobin (Mb) using multifaceted spectroscopic/voltammetric and docking techniques. The Mb-binding capacity of these geminis decreased in the order of C14-E2O-C14 > C16-E2O-C16 > C12-E2O-C12, following the 1:2 stoichiometry, as confirmed by the quantitative evaluation of binding constants via intrinsic fluorescence and cyclic voltammetry. The binding-induced microenvironmental and conformational changes of Mb were explored by pyrene/synchronous/three-dimensional (3-D) fluorescence and absorption spectroscopy. Furthermore, far- and near-ultraviolet (UV) circular dichroism spectral results depicted discernible changes in both secondary and tertiary structures of Mb upon complexation with Cm-E2O-Cm. Molecular docking specified the binding site, and aromatic residues involved in the complexation. These investigations provide deeper insight into the structure-property relationships of biomacromolecules, and they will be useful in designing/selecting appropriate surfactants which, in turn, can facilitate the application of protein-surfactant mixtures in pharmaceutical, biological, and industrial fields.

Item Type: Article
Subjects: Q Science > QD Chemistry
Divisions: Faculties > Faculty of Science > Department of Chemistry
Depositing User: AMU Library
Date Deposited: 03 Feb 2018 05:46
Last Modified: 05 Feb 2018 04:20
URI: http://ir.amu.ac.in/id/eprint/11057

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