Spectroscopic and molecular modelling analysis of the interaction between ethane‐1, 2‐diyl bis(N, N‐dimethyl‐N‐hexadecylammoniumacetoxy)dichloride and bovine serum albumin. (31st March 2015)

• Record Type: Journal Article
• Authors: Patel, Rajan; Mir, Muzaffar Ul Hassan; Maurya, Jitendra Kumar; Singh, Upendra Kumar; Maurya, Neha; Parray, Mehraj ud din; Khan, Abbul Bashar; Ali, Anwar
• Is Part Of: Luminescence. Volume 30:Number 8(2015:Dec.)
• Page Start: 1233
• Page End: 1241
• Publication Date: 2015-03-31
• Subjects: 16‐E2‐16 -- quenching -- fluorescence -- hypsochromic shift -- docking; Luminescence -- Periodicals; Bioluminescence -- Periodicals; Chemiluminescence -- Periodicals; Luminescence -- Periodicals; 535.35
• DOI: 10.1002/bio.2886
• Languages: English
• ISSNs: 1522-7235

Abstract

Abstract: Several spectroscopic approaches namely fluorescence, time‐resolved fluorescence, UV‐visible, and Fourier transform infra‐red (FT‐IR) spectroscopy were employed to examine the interaction between ethane‐1, 2‐diyl bis( N, N ‐dimethyl‐ N ‐hexadecylammoniumacetoxy)dichloride (16‐E2‐16) and bovine serum albumin (BSA). Fluorescence studies revealed that 16‐E2‐16 quenched the BSA fluorescence through a static quenching mechanism, which was further confirmed by UV–visible and time‐resolved fluorescence spectroscopy. In addition, the binding constant and the number of binding sites were also calculated. The thermodynamic parameters at different temperatures (298 K, 303 K, 308 K and 313 K) indicated that 16‐E2‐16 binding to BSA is entropy driven and that the major driving forces are electrostatic interactions. Decrease of the α‐helix from 53.90 to 46.20% with an increase in random structure from 22.56 to 30.61% were also observed by FT‐IR. Furthermore, the molecular docking results revealed that 16‐E2‐16 binds predominantly by electrostatic and hydrophobic forces to some residues in the BSA sub‐domains IIA and IIIA. Copyright © 2015 John Wiley & Sons, Ltd.