Combined molecular docking and multi-spectroscopic investigation on the interaction between Eosin B and human serum albumin

Yang, Qiao; Zhou, Xi; Chen, Xingguo

doi:10.1016/j.jlumin.2010.10.033

Cited by 37 publications

(11 citation statements)

References 27 publications

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“…The slight blue shift of Trp fluorescence indicates that the polarity around the tryptophan residue decreases and the hydrophobicity increases [36]. In a word, the synchronous fluorescence spectra indicated that the conformation of BSA has been changed [31,37].…”

Section: Synchronous Fluorescence Spectra and CD Spectramentioning

confidence: 97%

Synthesis and luminescent properties of Tb(III) complex with a novel pyrazolone ligand and its interaction with bovine serum albumin

Yang

Tang

Zhang

2012

Journal of Molecular Structure

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Section: Synchronous Fluorescence Spectra and CD Spectramentioning

confidence: 97%

Synthesis and luminescent properties of Tb(III) complex with a novel pyrazolone ligand and its interaction with bovine serum albumin

Yang

Tang

Zhang

2012

Journal of Molecular Structure

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“…Nowadays, the domain model of HSA tertiary structure is accepted, according to which the molecule of HSA consists of 3 practically identical domains (I−III), each of them in turn consists of two subdomains (A and B). 9 The internal zone of each domain is composed of hydrophobic amino acid residues, and the external zone of each domain consists of hydrophilic amino acid residues. The domains are placed at angles to each other, and their mutual relationships are described by a model in the shape of a heart.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Human serum albumin (HSA) is the most important and abundant constituent of blood plasma, which is a globular protein composed of 585 amino acid residues in a single polypeptide chain cross-linked with 17 disulfide bonds. Nowadays, the domain model of HSA tertiary structure is accepted, according to which the molecule of HSA consists of 3 practically identical domains (I–III), each of them in turn consists of two subdomains (A and B) . The internal zone of each domain is composed of hydrophobic amino acid residues, and the external zone of each domain consists of hydrophilic amino acid residues.…”

Section: Introductionmentioning

confidence: 99%

Probing the Binding of the Flavonoid Diosmetin to Human Serum Albumin by Multispectroscopic Techniques

Zhang

Wang

Pan

2012

J. Agric. Food Chem.

208

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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 indicated site I as the main binding site for diosmetin on HSA. The binding distance between diosmetin and HSA was determined to be 3.54 nm based on the Förster theory. Analysis of CD and FT-IR spectra demonstrated that HSA conformation was slightly altered in the presence of diosmetin.

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“…Processes such as absorption, excretion, and toxicity of drugs, for instance, during chemotherapy [ 1 ]—can be affected by the binding of these compounds with HSA [ 2 , 3 ]. Several investigations from experimental and theoretical [ 4 – 7 ] viewpoints on the binding of HSA with drugs have been performed. Some used drugs were 3′-azido-3′-deoxythymidine (AZT), aspirin, taxol, cisplatin, atrazine, 2,4-dichlorophenoxyacetic (2,4-D), polyamines, chlorophyll, chlorophyllin, poly(ethylene glycol), vanadyl cation, vanadate anion, cobalt-hexamine, and arsenic trioxide (As 2 O 3 ), astilbin [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Morphological Analysis and Interaction of Chlorophyll and BSA

Gorza

Pedro

Trescher

et al. 2014

BioMed Research International

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Interactions between proteins and drugs, which can lead to formation of stable drug-protein complexes, have important implications on several processes related to human health. These interactions can affect, for instance, free concentration, biological activity, and metabolism of the drugs in the blood stream. Here, we report on the UV-Visible spectroscopic investigation on the interaction of bovine serum albumin (BSA) with chlorophyll (Chl) in aqueous solution under physiological conditions. Binding constants at different temperatures—obtained by using the Benesi-Hildebrand equation—were found to be of the same order of magnitude (~104 M−1) indicating low affinity of Chl with BSA. We have found a hyperchromism, which suggested an interaction between BSA and Chl occurring through conformational changes of BSA caused by exposition of tryptophan to solvent. Films from BSA and Chl obtained at different Chl concentrations showed fractal structures, which were characterized by fractal dimension calculated from microscopic image analysis.

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Combined molecular docking and multi-spectroscopic investigation on the interaction between Eosin B and human serum albumin

Cited by 37 publications

References 27 publications

Synthesis and luminescent properties of Tb(III) complex with a novel pyrazolone ligand and its interaction with bovine serum albumin

Synthesis and luminescent properties of Tb(III) complex with a novel pyrazolone ligand and its interaction with bovine serum albumin

Probing the Binding of the Flavonoid Diosmetin to Human Serum Albumin by Multispectroscopic Techniques

Morphological Analysis and Interaction of Chlorophyll and BSA

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