Publications by authors named "Mehraj Ud Din Parray"

In this study, the complexation of potential chemo-therapeutic antibacterial drug, ciprofloxacin (CIP) with varying concentrations of surface active compounds (SACs) i.e., (N-(2-hydroxyethyl)-N,N-dimethyl-1-dodecanaminium bromide (12Cho.

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Herein, we have shown the interaction of levofloxacin (LVF) with two imidazolium based ionic liquids (ILs), 1-butly-3-methylimidazolium chloride ([Bmim][Cl]) and 1-decyl-3-methylimidazolium chloride ([Dmim][Cl]) by utilising spectroscopic techniques along with computational approach. Both [Bmim][Cl] and [Dmim][Cl] quenched the fluorescence emission of LVF suggesting complex formation between ILs and the drug. The steady-state and time-resolve fluorescence studies revealed that the quenching of fluorescence emission of LVF in the presence of [Bmim][Cl] and [Dmim][Cl], which signified the non-fluorescent complex formation between LVF and ILs.

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The present work is a brief overview of the effect of psychostimulant drug mephedrone hydrochloride (4MMC) on a transport protein, bovine serum albumin (BSA). The binding effect of 4MMC on BSA has been investigated by using UV-visible, steady-state fluorescence, time-resolved fluorescence, fluorescence resonance energy transfer, Fourier transform infrared, circular dichroism, and molecular docking method. 4-Methylmephedrone quenched the intrinsic fluorescence of BSA by static quenching mechanism, which was further confirmed by time-resolved fluorescence.

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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.

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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.

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