Intermolecular investigation on interaction of two ternary copper(II) Schiff base complexes with bovine serum albumin

Dezhampanah, Hamid; Firouzi, Roghaye; Shoeili, Zeinab Moradi; Binazir, Reihaneh

doi:10.1016/j.molstruc.2019.127557

Cited by 37 publications

(16 citation statements)

References 26 publications

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“…[17] This investigation might be very useful in supporting the relevance of medical communication. [18] In addition, we aimed to alert consumers to the quality of animal-derived food and strengthen supervision of food safety by relevant departments.…”

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confidence: 99%

Assessment on the binding characteristics of residual marbofloxacin in animal‐derived food to bovine/human serum albumin by spectroscopy and molecular modelling

Yue

Zhao

et al. 2021

Luminescence

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To assess the toxicity of residual marbofloxacin from animal-derived food, the interaction characteristics of marbofloxacin to bovine/human serum albumins (BSA/HSA) were explored using spectroscopic methods combined with molecular modelling.According to fluorescence spectra and time-resolved fluorescence spectra measurements, quenching of BSA/HSA fluorescence induced by marbofloxacin was characterized as static quenching. A 1:1 ground-state complex of marbofloxacin to BSA/HSA was formed with binding constant (K a ) 1.66 × 10 4 /9.74 × 10 3 M −1 at 291 K. The location of marbofloxacin binding at site I within BSA/HSA was clarified by site marker competitive experiments. Molecular modelling demonstrated that the binding region for marbofloxacin to BSA and HSA were at site I with the lowest binding free energies of −22.86 and −21.60 kJ mol −1 , respectively. Hydrogen bonds and van der Waals forces were dominantly involved in the spontaneous binding. Nonradiation energy transferred from BSA and HSA to marbofloxacin, due to the close distance (r 0 ) between marbofloxacin and Trp residues of BSA (4.28 nm) and HSA (3.34 nm). As explained by circular dichroism (CD) spectra, an increased BSA/HSA α-helix structure was observed after binding to marbofloxacin. Ultraviolet-visible (UV-vis) and Fourier transform infrared (FT-IR) spectra suggested that conformation of the two proteins was altered by marbofloxacin.

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confidence: 99%

Assessment on the binding characteristics of residual marbofloxacin in animal‐derived food to bovine/human serum albumin by spectroscopy and molecular modelling

Yue

Zhao

et al. 2021

Luminescence

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“…The shorter distance indicated the greater binding force. [ 29,46 ] Thus H‐bonding interaction existed in the complexes of CYP2D6‐astilbin, CYP2D6‐isoastilbin and CYP2D6‐neoastilbin. The hydrophobic interaction between the benzene ring and hydrophobic residues was also observed due to the distribution of astilbin, isoastilbin, neoastilbin near the hydrophobic region.…”

Section: Resultsmentioning

confidence: 99%

Interaction study of astilbin, isoastilbin and neoastilbin toward CYP2D6 by multi‐spectroscopy and molecular docking

et al. 2021

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Astilbin, isoastilbin and neoastilbin are the three flavonoid isomers prevalent in Rhizoma Smilax glabra. The interactions between human cytochrome P450 2D6 (CYP2D6) and the three isomers were investigated by multiple spectroscopic coupled with molecular docking. As a result, the fluorescence intensity of CYP2D6 was quenched statically by the three isomers. Meanwhile, astilbin had the strongest binding ability to CYP2D6, followed by isoastilbin and neoastilbin under the identical temperature. Synchronous fluorescence, three‐dimensional fluorescence, ultraviolet‐visible spectroscopy, circular dichroism and Fourier‐transform infrared spectra confirmed that the conformation and micro‐environment of CYP2D6 protein were changed after binding with the three isomers. As suggested from molecular docking, the three isomers had strong binding affinity to CYP2D6 via the bonding of hydrogen and van der Waals forces, and the results were in agreement with the fluorescence results. The findings here suggested that astilbin, isoastilbin and neoastilbin may cause the herb–drug interactions for their inhibition of CYP2D6 activity.

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“…28 According to the formula, the Stern-Volmer (S-V) curve of β-CN interacting with FLU and PIT were in a linear relationship (Fig. 1) 29 also, with the use of the equation we observed that kq for complex FLU-β-CN and PIT-β-CN is 1.6×10 13 and 1.45×10 13 M -1 S -1 respectively that is greater than the maximum diffusion collision quenching rate constant (2.0×10 10 M -1 S -1 ), these results indicate that the static quenching effect exists in the system of FLU and PIT with β-CN. 30,31 For the quenching process of β-CN, the binding constant (Kb) of a complex of FLU and PIT with β-CN can be determined by the following equation (3) (Fig.…”

Section: Accepted Manuscriptmentioning

confidence: 96%

Binding of β-casein with fluvastatin and pitavastatin

Dezhampanah

Rajabi

2022

JSCS

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In this work, the binding interaction of fluvastatin (FLU) and pitavastatin (PIT) with bovine ?-casein (?-CN) were performed under physiological conditions (pH 7.2) by fluorescence emission spectroscopy, synchronous fluorescence spectroscopy, Fourier transform infrared spectroscopy (FTIR) and molecular docking methods. Due to the formation of FLU-?-CN and PIT-?-CN complexes, the intrinsic fluorescence of ?-CN was quenched. The number of bound FLU and PIT per protein molecule (n) were about 1, also the binding constant of FLU-?-CN and PIT-?-CN complexes were 7.96?104 and 3.44?104M-1 at 298 K, respectively. This result suggests that the binding affinity of FLU to ?-CN was higher than that for PIT. Molecular modeling showed different binding sites for FLU and PIT on ?-CN. All these experimental results suggest that ?.

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Intermolecular investigation on interaction of two ternary copper(II) Schiff base complexes with bovine serum albumin

Cited by 37 publications

References 26 publications

Assessment on the binding characteristics of residual marbofloxacin in animal‐derived food to bovine/human serum albumin by spectroscopy and molecular modelling

Assessment on the binding characteristics of residual marbofloxacin in animal‐derived food to bovine/human serum albumin by spectroscopy and molecular modelling

Interaction study of astilbin, isoastilbin and neoastilbin toward CYP2D6 by multi‐spectroscopy and molecular docking

Binding of β-casein with fluvastatin and pitavastatin

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