The binding mechanism of molecular interaction between diosmetin and human serum albumin (HSA) in a pH 7.4 phosphate buffer was studied using atomic force microscopy (AFM) and various spectroscopic techniques including fluorescence, resonance light scattering (RLS), UV–vis absorption, circular dichroism (CD), and Fourier transform infrared (FT–IR) spectroscopy. Fluorescence data revealed that the fluorescence quenching of HSA by diosmetin was a static quenching procedure. The binding constants and number of binding sites were evaluated at different temperatures. The RLS spectra and AFM images showed that the dimension of the individual HSA molecules were larger after interaction with diosmetin. The thermodynamic parameters, ΔH° and ΔS° were calculated to be −24.56 kJ mol–1 and 14.67 J mol–1 K–1, respectively, suggesting that the binding of diosmtin to HSA was driven mainly by hydrophobic interactions and hydrogen bonds. The displacement studies and denaturation experiments in the presence of urea indicate...

Probing the binding of the flavonoid diosmetin to human serum albumin by multispectroscopic techniques.

Recent advances in applications of single-drop microextraction: A review

New developments in microextraction techniques in bioanalysis. A review.

Inhibitory effect of phloretin on α-glucosidase: Kinetics, interaction mechanism and molecular docking.

Herein, we report the interaction of synthesized pyrrolidinium based ionic liquid, N-butyl-N-methyl-2-oxopyrrolidinium bromide (BMOP) with human serum albumin (HSA). The BMOP was characterized by using 1H NMR, 13C NMR and FT-IR techniques. The critical micelle concentration (cmc) of BMOP was confirmed by surface tension, conductivity and contact angle measurements. The interactions between HSA and BMOP were studied by steady-state and time-resolved fluorescence, UV–visible, FT-IR spectroscopic and molecular docking methods. The steady-state fluorescence spectra showed that BMOP quenched the fluorescence of HSA through combined quenching mechanism. Corresponding thermodynamic parameters viz. Gibbs free energy change (ΔG), entropy change (ΔS) and enthalpy change (ΔH) illustrated that the binding process was spontaneous and entropy driven. It is also suggested that hydrophobic forces play a key role in the binding of BMOP to HSA. In addition, the pyrene probe analysis again suggests the involvement of hydrophobic interaction in HSA–BMOP complex formation. Surface tension profile showed that the cmc value of BMOP in the presence of HSA is higher than the cmc value of pure BMOP. The FT-IR results show a conformational change in the secondary structure of HSA upon the addition of BMOP. The molecular docking result indicated that BMOP binds with HSA at hydrophobic pocket domain IIA with hydrophobic and hydrogen bond interactions in which hydrophobic interactions are dominating.

Nana Li

Papers

The interaction of 2-mercaptobenzimidazole with human serum albumin as determined by spectroscopy, atomic force microscopy and molecular modeling.

Study of interaction between syringin and human serum albumin by multi-spectroscopic method and atomic force microscopy

Selective extraction of alkaloids in human urine by on-line single drop microextraction coupled with sweeping micellar electrokinetic chromatography.

Binding studies of costunolide and dehydrocostuslactone with HSA by spectroscopy and atomic force microscopy