Multi‐Spectroscopic and Theoretical Analyses of Human Serum Albumin Binding to a Water‐Soluble Zinc(II) Complex including β‐Amino Alcohol

Abstract

In this study, we examined the interaction process of human serum albumin (HSA) with a water-soluble zinc(II) complex of dichloro {2-[N-(2-hydroxyethylammonioethyl) imino methyl] phenol} at pH = 7.4 and in vitro utilizing molecular docking modeling and spectral techniques. In the multi-temperature fluorescence test, the consecutive and gradual addition of the zinc(II) complex to the HSA-containing cell resulted in fluorescence quenching, and it showed that the zinc(II) complex-protein interaction is associated with a static quenching mechanism; also, the number of binding sites (n) and the binding constant (K b ) were computed by this test. The evaluation of thermodynamic data showed spontaneous progression, and the involvement of hydrogen bonding/van der Waals forces in protein-zinc(II)complex formation. The site markers competition studies using two drugs, warfarin and ibuprofen, indicated that zinc(II) complex binds to the protein via site I/sub-domain IIA. The albumin-zinc(II) complex interaction and the structural alterations in the serum albumin were proved by electronic absorption technique and circular dichroism spectroscopy. Job's curve exhibited a stoichiometric ratio of 1 : 1 in the HSA-zinc(II) complex adduct. The accuracy of the results obtained from experimental findings on the interaction between HSA and zinc(II) complex was checked by molecular docking simulation, which illustrated a good agreement between experimental and theoretical data.

Coordination of an amino alcoholic Schiff base ligand toward the zinc(II) ion: spectral, structural, theoretical, and docking studies

“…Study of the IR spectrum of 1 revealed that there are different types of moieties in this structure for example, ν (C−H) aromatic, ν (O−H) alcoholic and ν (N−H) amine at above 3000 cm −1 , ν (C−H) aliphatic at near 3000 cm −1 and ν (C=N) imine at near 1550 cm −1 . A peak corresponding to the amine group is shifted 59 cm −1 to lower frequencies respect to the free ligand [31]. This shifts have been reported previously for alkylammonium ions [32,33] and confirming the formation of zwitterionic form of ligand.…”

“…All starting chemicals and solvents (Merck, Aldrich) were used as received without further purification. The L ligand was prepared as described in previous work [31]. The infrared spectrum (as KBr pellet) in the range 400-4000 cm -1 was recorded with a Shimadzu FT-IR 8400 spectrometer.…”

Effect of Steam Flash-Explosion on Physicochemical Properties and Structure of High-Temperature Denatured Defatted Rice Bran Protein Isolate

“…According to the method of Shahabadi et al [ 43 ], a certain amount of RBPI was accurately measured by freeze-dried samples and dissolved in 10 mmol/L pH 7.0 phosphate buffer to prepare 0.2 mg/mL protein solution. The solution was measured on a circular dichroic spectrometer (J-810, Japan Spectroscopic JASCO Corporation, Tokyo, Japan).…”