The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study

Sengupta, Bidisa; Sengupta, Pradeep K.

doi:10.1016/s0006-291x(02)02667-0

Cited by 203 publications

(154 citation statements)

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“…15) In the present experiments, the binding constants of IVIG with kaempferol and quercetin calculated are 1.032ϫ10 4 M Ϫ1 and 1.849ϫ10 4 M Ϫ1 (nϭ2) at 296 K, respectively. These indicate that the bindings of HSA to kaempferol and quercetin are stronger than that of IVIG to them, and there will be a competitive reaction between HSA and IVIG binding to kaempferol and quercetin in blood.…”

mentioning

confidence: 47%

“…1) and other related plant flavonols have come into recent prominence because of their usefulness as anticancer, antitumor, anti-AIDS, and other important therapeutic activities of significant potency and low systemic toxicity. [15][16][17][18] It is non-specific and reversible that many of these agents bind to serum proteins, and the binding affects their pharmacological and pharmacokinetic properties.…”

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confidence: 99%

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Study on the Interactions of Kaempferol and Quercetin with Intravenous Immunoglobulin by Fluorescence Quenching, Fourier Transformation Infrared Spectroscopy and Circular Dichroism Spectroscopy

Zhou

Yao

et al. 2008

CHEMICAL & PHARMACEUTICAL BULLETIN

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Initially used as replacement therapy for patients with primary and secondary immune deficiencies, intravenous immunoglobulin (IVIG), the human serum immunoglobulin (Ig) fraction that is mainly composed of normal human polyclonal IgG obtained from plasma pools from a large number of healthy blood donors, is now widely used for the treatment of a large number of autoimmune and systemic inflammatory diseases. 1,2) Recently, great attention has been paid to IVIG potential use as adjuvant anti-neoplastic agent.3-5) Studies on the anticancer alkaloid vindesine (VDS) conjugates of the anti-CEA (carcinoembryonic antigen) antibodies against a colorectal tumor xenograft revealed that antibody 14.95.55 (IgG2a) suppressed tumor growth both alone and as a VDS conjugate, while 11.285.14 (IgG1) produced only a slight effect alone but an almost complete and lasting suppression of tumor growth as a VDS conjugate. Acute studies showed that VDS-11.285.14 conjugate was considerably less toxic than free VDS in Balb/c mice.6) It has been revealed that there are different transfer mechanism between the drug-protein conjugates and free drugs transferred into cells, and the conjugates can reduce the toxicity of drugs, resulting in a prolongation of survival time.7) Studies on the efficacy of an IgG F(ab) 2 preparation against taxol-induced C activation revealed that at a therapeutically relevant dose level (10 mg/ml), this Fc-depleted IgG caused significant suppression of taxol-induced SC5b-9 formation, but replacing IVIG with 10 mg/ml human serum albumin (HSA) caused no inhibition of taxolinduced rise of SC5b-9. 8) Also, it is reported that within a range of molar concentration ratio of taxol to IVIG, the interaction of IVIG with taxol can inhibit taxol from crystallizing in aqueous solution.9) Studies in vitro have revealed that IVIG may stimulate the production of IL-12, an anti-tumor and anti-angiogenic cytokine, and enhanced NK cell activity.4) Studies also revealed that IVIG can decrease the level of matrix metalloproteinase-9 (MMP-9) expression in the U937 monocyte line with a decrease in the m-RNA level of MMP-9 that participates in basement membrane degradation, a vital step in the invasion of metastatic cancer cells. So, IVIG may serve as an adjuvant therapy in cancer due to its anti-neoplastic properties that may synergize with more specific MMP inhibitors and other anti-cancer drugs. 10,11) In addition, IgG presents itself in the blood of adults at 9.5-12.5 mg/ml, and as one of human plasma proteins, it is capable of binding an extraordinarily diverse range of metabolites, drugs, organic compounds and relevant antigens. [12][13][14] With the remarkable binding properties, IVIG can serve as an important transport protein for drugs, which may have important roles in the discovery of novel drug delivery system and targeted drug therapy. By using its high-safety profile, clinicians may construct new protocols for patients.Flavonols are plant pigments that are ubiquitous in nature. Kaempferol (3,4Ј,5,7-pentahydroxyflavone), quer...

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confidence: 47%

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confidence: 99%

Study on the Interactions of Kaempferol and Quercetin with Intravenous Immunoglobulin by Fluorescence Quenching, Fourier Transformation Infrared Spectroscopy and Circular Dichroism Spectroscopy

Zhou

Yao

et al. 2008

CHEMICAL & PHARMACEUTICAL BULLETIN

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“…• C in the seminal paper by Sengupta and Sengupta [7]. The standard Gibbs free energy change of binding quercetin to albumin was found to be approximately 32 kJ/mol at 37…”

Section: Resultsmentioning

confidence: 99%

“…In recent few years, great attention has been paid to the study of avonoids [7]. They are known to show biological activity.…”

Section: Introductionmentioning

confidence: 99%

Optical Spectroscopy Study of the Interaction Between Quercetin and Human Serum Albumin

Wybranowski¹,

Kruszewski²

2014

Acta Phys. Pol. A

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Optical methods are very useful for the study on behavior of molecules in albumin-containing solutions. The interaction between quercetin (QUE) and human serum albumin (HSA) under physiological conditions was investigated by the methods of UV-Vis absorption and uorescence spectroscopy. Fluorescence data show that enhancing of quercetin uorescence in the presence of HSA is the result of formation of the HSA-QUE complex. On the basis of uorescence data, the binding anity constant of quercetin to HSA is determined. In this paper we have attempted to perform a kinetic study of the oxidation of quercetin in presence of human serum albumin by absorption spectroscopy. It has been shown that quercetin easily oxidizes at pH 7.4. The addition of HSA to quercetin solution induces changes in the absorption spectrum. In the human serum albumin solution, the time of quercetin oxidation is longer than in the case of quercetin diluted in phosphate buered saline. Human albumin also contributes to stabilization of quercetin. These results suggest that HSA prevents degradation of quercetin in blood.

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“…Up to now, extensive investigations into interactions between protein and internal compounds or pharmaceutical molecules have been stimulated. [11][12][13][14][15][16] This is because information concerning the interaction of serum albumin and a drug can help us to better understand the interaction mechanism and the absorption, as well as the distribution and toxicity of drugs. Molecular interactions are often monitored by optical techniques.…”

Section: N-(p-ethoxy-phenyl)-n′-(1-naphthyl)thioureamentioning

confidence: 99%

Binding of Human Serum Albumin to N-(p-Ethoxy-phenyl)-N′-(1-naphthyl)thiourea and Synchronous Fluorescence Determination of Human Serum Albumin

et al. 2007

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The binding of N- (p-ethoxy-phenyl)-N′-(1-naphthyl)thiourea (EPNT) to human serum albumin (HSA) was investigated under simulative physiological conditions by fluorescence spectra in combination with UV absorption spectroscopy and a molecular modeling method. A strong fluorescence quenching reaction of EPNT to HSA was observed, and the quenching mechanism was suggested to be static quenching according to the Stern-Volmer equation. The binding constants (K) at different temperatures as well as thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated according to relevant fluorescent data and the vant' Hoff equation. This indicated that a hydrophobic interaction was a predominant intermolecular force for stabilizing the complex, which is in agreement with the results of molecule modeling study. The effects of energy transfer and other ions on the binding constant were considered. In addition, synchronous fluorescence technology was successfully applied to the determination of HSA added into the EPNT solution.

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The interaction of quercetin with human serum albumin: a fluorescence spectroscopic study

Cited by 203 publications

References 20 publications

Study on the Interactions of Kaempferol and Quercetin with Intravenous Immunoglobulin by Fluorescence Quenching, Fourier Transformation Infrared Spectroscopy and Circular Dichroism Spectroscopy

Study on the Interactions of Kaempferol and Quercetin with Intravenous Immunoglobulin by Fluorescence Quenching, Fourier Transformation Infrared Spectroscopy and Circular Dichroism Spectroscopy

Optical Spectroscopy Study of the Interaction Between Quercetin and Human Serum Albumin

Binding of Human Serum Albumin to N-(p-Ethoxy-phenyl)-N′-(1-naphthyl)thiourea and Synchronous Fluorescence Determination of Human Serum Albumin

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