Publications by authors named "Muzaffar Ul Hassan Mir"

The refolding of urea denatured horse heart cytochrome c (h-cyt-c) under the influence of ester based cationic gemini surfactants [ethane-1, 2-diyl bis(N, N-dimethyl-N-alkylammoniumacetoxy) dichlorides] 16-E2-16, 14-E2-14 and 12-E2-12 (n-E2-n) was performed by using UV-visible, fluorescence and circular dichroism (CD) spectroscopic techniques. We found that n-E2-n geminis promote the formation of molten globule (MG) like state upon addition into the urea denatured h-cyt-c. The comparative study of refolding of denatured h-cyt-c with n-E2-n, cationic gemini surfactant show stabilization of MG-like state influenced by hydrophobic interactions.

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The interactions of imidazolium bashed ionic liquid-type cationic gemini surfactant ([C12-4-C12im]Br2) with HSA were studied by fluorescence, time-resolved fluorescence, UV-visible, circular dichroism, molecular docking and molecular dynamic simulation methods. The results showed that the [C12-4-C12im]Br2 quenched the fluorescence of HSA through dynamic quenching mechanism as confirmed by time-resolved spectroscopy. The Stern-Volmer quenching constant (Ksv) and relevant thermodynamic parameters such as enthalpy change (ΔH), Gibbs free energy change (ΔG) and entropy change (ΔS) for interaction system were calculated at different temperatures.

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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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Herein, we are reporting the interaction of ionic liquid type gemini surfactant, 1,4-bis(3-dodecylimidazolium-1-yl) butane bromide ([C12-4-C12 im]Br2) with lysozyme by using Steady state fluorescence, UV-visible, Time resolved fluorescence, Fourier transform-infrared (FT-IR) spectroscopy techniques in combination with molecular modeling and docking method. The steady state fluorescence spectra suggested that the fluorescence of lysozyme was quenched by [C12-4-C12 im]Br2 through static quenching mechanism as confirmed by time resolved fluorescence spectroscopy. The binding constant for lysozyme-[C12-4-C12 im]Br2 interaction have been measured by UV-visible spectroscopy and found to be 2.

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