Interaction of promethazine and adiphenine to human hemoglobin: A comparative spectroscopic and computational analysis.

Autor: Maurya N; Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi 110025, India., Ud Din Parray M; Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi 110025, India., Maurya JK; Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi 110025, India., Kumar A; Centre for Nano and Material Sciences, Jain University, Jain Global Campus, Jakkasandra Post, Bangalore 562112, India., Patel R; Biophysical Chemistry Laboratory, Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia (A Central University), New Delhi 110025, India. Electronic address: rpatel@jmi.ac.in.
Jazyk: angličtina
Zdroj: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy [Spectrochim Acta A Mol Biomol Spectrosc] 2018 Jun 15; Vol. 199, pp. 32-42. Date of Electronic Publication: 2018 Mar 11.
DOI: 10.1016/j.saa.2018.03.023
Abstrakt: The binding nature of amphiphilic drugs viz. promethazine hydrochloride (PMT) and adiphenine hydrochloride (ADP), with human hemoglobin (Hb) was unraveled by fluorescence, absorbance, time resolved fluorescence, fluorescence resonance energy transfer (FRET) and circular dichroism (CD) spectral techniques in combination with molecular docking and molecular dynamic simulation methods. The steady state fluorescence spectra indicated that both PMT and ADP quenches the fluorescence of Hb through static quenching mechanism which was further confirmed by time resolved fluorescence spectra. The UV-Vis spectroscopy suggested ground state complex formation. The activation energy (E a ) was observed more in the case of Hb-ADP than Hb-PMT interaction system. The FRET result indicates the high probability of energy transfer from β Trp37 residue of Hb to the PMT (r=2.02nm) and ADP (r=2.33nm). The thermodynamic data reveal that binding of PMT with Hb are exothermic in nature involving hydrogen bonding and van der Waal interaction whereas in the case of ADP hydrophobic forces play the major role and binding process is endothermic in nature. The CD results show that both PMT and ADP, induced secondary structural changes of Hb and unfold the protein by losing a large helical content while the effect is more pronounced with ADP. Additionally, we also utilized computational approaches for deep insight into the binding of these drugs with Hb and the results are well matched with our experimental results.
(Copyright © 2018 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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