The interaction between 4-aminoantipyrine and bovine serum albumin: Multiple spectroscopic and molecular docking investigations

Teng, Yue; Liu, Rutao; Li, Chao; Xia, Qing; Zhang, Pengjun

doi:10.1016/j.jhazmat.2011.03.084

Cited by 86 publications

(27 citation statements)

References 50 publications

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“…Due to the high rate of decrease of K a in the competitive assays as other competitive probes [35], it could be deduced that chrysin may possessed a matched ability to compete with allopurinol for the same binding site which was proved to be the active cavity of XO. Allopurinol with the same concentration had a little effect on the K a of apigenin-XO complex (from 1.10 × 10 4 to 1.07 × 10 4 L mol −1 ), implying that apigenin could not compete the same binding site with allopurinol.…”

Section: Binding Constant and Binding Sitementioning

confidence: 99%

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism

Lin

Zhang

Liao

et al. 2015

International Journal of Biological Macromolecules

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Section: Binding Constant and Binding Sitementioning

confidence: 99%

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism

Lin

Zhang

Liao

et al. 2015

International Journal of Biological Macromolecules

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“…Moreover, it has two tryptophan residues (Trp134 and Trp212), that is to say, Trp-134 in the first domain is located on the surface of the molecule, and Trp-212 in the second domain is located within a hydrophobic binding pocket of BSA, whereas, HSA consists of a single polypeptide chain with 585 amino acid residues in which the single tryptophan residue (Trp214) measures the drug-binding affinity [4,5]. For many years, the interactions between SAs and small molecular probes have attracted a great deal of interest due to their application in a great variety of biological, pharmaceutical, toxicological and cosmetic systems [6]. However, the strong binding of drug to protein can decrease the concentration of free drug in plasma, whereas the weak binding can lead to a short lifetime or poor distribution.…”

Section: Introductionmentioning

confidence: 99%

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Cheng

2012

Mol Biol Rep

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This study was designed to examine the interactions of ergosterol with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with the drug concentrations in the range of 2.99-105.88 μM and the concentration of proteins was fixed at 5.0 μM. The analysis of emission spectra quenching at different temperatures revealed that the quenching mechanism of HSA/BSA by ergosterol was the static quenching. The number of binding sites n and the binding constants K were obtained at various temperatures. The distance r between ergosterol and HSA/BSA was evaluated according to Föster non-radioactive energy transfer theory. The results of synchronous fluorescence, 3D fluorescence, FT-IR, CD and UV-Vis absorption spectra showed that the conformations of HSA/BSA altered in the presence of ergosterol. The thermodynamic parameters, free energy change (ΔG), enthalpy change (ΔH) and entropy change (ΔS) for BSA-ergosterol and HSA-ergosterol systems were calculated by the van't Hoff equation and discussed. Besides, with the aid of three site markers (for example, phenylbutazone, ibuprofen and digitoxin), we have reported that ergosterol primarily binds to the tryptophan residues of BSA/HSA within site I (subdomain II A).

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“…There exist three similar domains (I, II, and III) in structure of BSA, which are typically bound reversibly with ligands (Paul, et al, 2010;Teng et al, 2011). The ligands can simultaneously bind to BSA by competitive binding and non-competitive binding mechanism.…”

Section: Binding Mode and Binding Site Between Triptolide And Bsa Sitmentioning

confidence: 99%

Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods

Wang¹,

Shi²,

Pang³

et al. 2016

Afr J Tradit Complement Altern Med

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Background: Triptolide is a major active constituent isolated from Tripterygiumwilfordii Hook F, a Chinese herbal medicine. This study investigated the intermolecular interaction between triptolide and bovine serum albumin (BSA). Materials and Methods:The fluorescence, circular dichroism (CD) and molecular docking methods were used to investigate the intermolecular interaction between triptolide and BSA. The binding constant, the number of binding sites, binding subdomain and the thermodynamic parameters were measured. Results: The results of this experiment revealed that the intrinsic fluorescence of BSA was effectively quenched by triptolide via static quenching. The experimental results of synchronous fluorescence and CD spectra showed that the conformation of BSA was changed in the presence of triptolide. Conclusion: It indicated that triptolide could spontaneously bind on site II (subdomain IIIA) of BSA mainly via hydrogen bonding interactions and Van der Waals force.

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The interaction between 4-aminoantipyrine and bovine serum albumin: Multiple spectroscopic and molecular docking investigations

Cited by 86 publications

References 50 publications

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism

Inhibition of chrysin on xanthine oxidase activity and its inhibition mechanism

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

Studies on the Interaction Between Triptolide and Bovine Serum Albumin (Bsa) by Spectroscopic and Molecular Modeling Methods

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