Spectrometric and voltammetric studies of the interaction between quercetin and bovine serum albumin using warfarin as site marker with the aid of chemometrics

Ni, Yongnian; Zhang, Xia; Kokot, Serge

doi:10.1016/j.saa.2008.07.004

Cited by 119 publications

(89 citation statements)

References 36 publications

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“…7 In other words, the absorption of the B ring was due to Band I in the 320-385 nm range, while A ring absorption would be responsible for band II (250-285 nm). UV-visible spectra of the complexed chemicals (quercetin and luteolin respectively with BSA) showed an increase in the UV absorbance intensity of BSA with increasing concentration of both flavonoids.…”

Section: Resultsmentioning

confidence: 99%

“…Further, our report has specifically documented a hitherto unreported UV-visible spectroscopy-based 3 and 4.1 nm shifts for luteolin and quercetin respectively. Ni et al, 2009 7 adopted a different experimental design in terms of keeping the concentrations of both quercetin (16.5 µM) and BSA (15.0 µM) constant. They have reported a qualitatively similar hypsochromic shift with respect to BSA.…”

Section: Discussionmentioning

confidence: 99%

“…16 Fluorescence spectroscopy results seem to point towards a static quenching mechanism under our defined experimental conditions (Table 1a and 1b). 5,7,8,10,13,14,17 There have been very few reports wherein a comparison has been made between luteolin and quercetin with respect to fluorescence spectroscopy data. 13,17 Unlike the experimental flow in these reports, we have adopted an experimental design wherein thermodynamic and docking data have also been incorporated (please see below).…”

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confidence: 99%

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A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Krishnan¹,

Hiray²,

Vyas³

2018

IJPER

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The in vitro in silico experimental flow (multi-spectroscopy and docking) demonstrated the binding of Luteolin and Quercetin separately with Bovine Serum Albumin. For the first time, we are reporting the relative UV-visible spectroscopy-based hypsochromic shifts for both luteolin (3nm) and quercetin (4.1 nm) respectively. The drug-induced conformational change may lead to the possible shift in the tryptophan residue to a more hydrophobic environment. Our demonstration of an increased static quenching of the endogenous fluorophore in BSA validated the UV-visible spectroscopy data. However, detailed experiments will further delineate the possible relative contribution of dynamic quenching processes. The strong binding (binding constant values -10 5 L/mol) and the number of binding sites (1 for luteolin and quercetin) is consistent with published findings. Under our defined conditions, the hitherto unreported non-cooperative binding was demonstrated, based on the Hill's coefficient. Thermodynamic data qualitatively validated hydrophobicity (a positive entropy change ΔS 0 ); hydrogen bonding (a negative ΔH 0 ) and electrostatic interactions (a negative ΔH 0 and a positive ΔS 0 ). For the first time, the Infra-Red Spectroscopy (FT-IR) data showed ground state complex formation of the molecules with the model protein and may serve to corroborate our fluorescence (static quenching) data. Hydrogen bonds and hydrophobic interactions for both molecules (Ligplot Analysis) provide corroborative evidence for the molecular spectroscopy and thermodynamic data. This hitherto unreported, unique, combinatorial in vitro (multispectroscopy and thermodynamic measurements) in silico (docking and Ligplot-based analysis) experimental flow (specifically for luteolin and quercetin) provides a basis for extending such binding studies for novel receptors and/or ligands.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Krishnan¹,

Hiray²,

Vyas³

2018

IJPER

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“…Many research groups have studied the in vivo consequences of binding of drugs and their metabolites to serum albumins (Lupidi et al, 2010;Yue et al, 2009). These researchers have examined the binding mechanisms of 1igands with serum albumin by using absorption (Tian et al, 2004), fluorescence and voltammetric techniques (Kitson, 2004;Dufour and Dangles, 2005;Nia et al, 2009;Choiprasert and Mankhetkorn, 2006). Based on these studies, the information on the binding processes of many exogenous ligands like long chain fatty acids, amino acids, drugs, bilirubin, etc.…”

Section: Introductionmentioning

confidence: 99%

“…The two serum albumins (HSA and BSA) have been shown to strongly bind quercetin and other structurally related flavonoids in vitro (Kitson, 2004;Dufour and Dangles, 2005;Nia et al, 2009;Choiprasert and Mankhetkorn, 2006). Dangles et al (1999) and Dufour and Dangles (2005) quantitatively measured the binding constant (K D ) of quercetin and its glycoside derivatives to BSA by using fluorescence spectroscopy, the determined K D values was equal to 8.6 (± 1.1) ×10 5 M −1 and 14.5 (± 2.8) ×10 5 M −1 for rutin and isoquercetrin, respectively.…”

Section: Introductionmentioning

confidence: 99%

Relation between Macroscopic Binding Constant and the Anticancer Efficacy of the Bovine Serum Albumin-Quercetin Complex against Drug-Sensitive and Drug-Resistant Cells

Choiprasert¹

2011

American Journal of Biochemistry and Biotechnology

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Problem statement:We have previously analyzed the interaction of BSA with flavonoids by using FRET. In this study, the role of BSA on increasing in solubility and on carrying the quercetin derivatives thus enhanced their anticancer efficacy against drug-sensitive and drug-resistant cells were conducted. ) at C3 yielded an increase in stability of the complexes. Rutin was tightly bound to BSA resulting in the changes in mode of action. Conclusion: The macroscopic binding constant was directly influenced on the cellular uptake of molecules and the suitable range of binding constant was K D ≥10 5 M −1 by which the carrier can be useful for increasing the solubility of drug and also spontaneously release the drug into the solution and cells.

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The influence of several nutritional supplements on the rational use of cabozantinib

Duan

Wang²,

Liu

et al. 2022

Luminescence

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To promote the rational use of cabozantinib (CBZ), this paper studied the influence of several nutritional supplements on the interaction between CBZ and bovine serum albumin (BSA), an appropriate alternative model for human serum albumin (HSA) that is one of the important transporter proteins in plasma, by fluorescence spectroscopy and UV–vis spectroscopy. The results showed that CBZ could quench the fluorescence of BSA via a dynamic–static quenching process, and the six nutritional supplements did not change the quenching mode of BSA by CBZ. However, all of them could reduce the binding constant of the CBZ–BSA system at 293 K and increase the polarity around tryptophan residues. Among them, nicotinamide and vitamin B12 (VB12) had a greater effect on the binding constants of the CBZ–BSA system. In the meantime, the thermodynamic parameters of the CBZ–BSA system were examined, indicating that the interaction of CBZ with BSA was spontaneous and dominated by hydrophobic forces. Further research discovered that the combining of CBZ with BSA was primarily located within Site I of BSA, and the binding distance r was 2.48 nm. Consequently, while taking CBZ, patients should use VB12 and nicotinamide carefully, which may interfere with the transport of drugs.

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Spectrometric and voltammetric studies of the interaction between quercetin and bovine serum albumin using warfarin as site marker with the aid of chemometrics

Cited by 119 publications

References 36 publications

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

A Correlative Multi-Spectroscopy and Docking Study for the Modeling of Drug (Luteolin and Quercetin) Binding to Bovine Serum Albumin– A Tool for the Determination of Binding Characteristics to Receptor Proteins

Relation between Macroscopic Binding Constant and the Anticancer Efficacy of the Bovine Serum Albumin-Quercetin Complex against Drug-Sensitive and Drug-Resistant Cells

The influence of several nutritional supplements on the rational use of cabozantinib

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