Study of the interaction of kaempferol with bovine serum albumin

Tian, Jianniao; Liu, Jiaqin; Tian, Xuan; Hu, Zhide; Chen, Xingguo

doi:10.1016/j.molstruc.2003.12.019

Cited by 125 publications

(68 citation statements)

References 25 publications

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“…As shown in Fig. 8a, , respectively, at 296 K. 17,18) A fluorescence spectroscopic study of the interaction of quercetin with HSA revealed that quercetin molecules bind at a motionally restricted site near tryptophan-214 in the intradomain cleft region of HSA, and the binding constant (Kϭ1.9ϫ10 5 …”

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confidence: 96%

“…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%

“…12) Therefore a study on the binding of 16,17) Furthermore, the interaction of IVIG with drugs in fact represents the behavior of IgG and it is of much more clinical use.…”

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confidence: 99%

“…Where K 2 is the orientation factor related to the geometry of the donor-acceptor of dipole and K 2 ϭ2/3 for random orientation as in fluid solution 17) ; n (ϭ1.336) is the refractive index of medium; F is the fluorescence quantum yield of the donor, its value was taken as 0. 118 27) ; J is the overlap integral of the fluorescence emission spectra of the donor and the absorption spectra of the acceptor.…”

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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: 96%

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confidence: 99%

“…12) Therefore a study on the binding of 16,17) Furthermore, the interaction of IVIG with drugs in fact represents the behavior of IgG and it is of much more clinical use.…”

mentioning

confidence: 99%

mentioning

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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“…Flavonoids especially kaempferol, were found to have inhibitory effects on trypsin as a result of their hydroxyl groups [27]. In serum albumin strongly by hydrophobic interactions and this resulted in changes in secondary structure of protein [22]. The enhanced enzyme activity due the higher temperatures should also increase the amount of precipitate formed.…”

Section: Trypsin Stability Studiesmentioning

confidence: 99%

Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract

Uslu¹,

Bayraktar²,

Ceylan³

2014

Turk J Bioch

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Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract [Trypsin ve Equisetum arvense özütü arasındaki etkileşimin kinetik ve yapısal karakterizasyonu] ABSTRACT Objective: In this study the inhibitory effect of E. arvense extract on trypsin activity and the effect of trypsin on E. arvense extract were studied. In addition the nature of the interaction between the extract and trypsin was investigated. Methods: The inhibitory effect ethanol extract of E. arvense on trypsin activity was determined using trypsin enzyme assay. The structural effects of the extract-trypsin interaction for the extract were analyzed by FTIR. Finally, the HPLC analyses were carried out to analyze the individual components of the extract and the supernatant and soluble precipitate phases. Results: E. arvense extract was found to decrease total percent activity of trypsin to 5% in 24 hour at 24 °C. FTIR analyses indicated that the interaction between trypsin and E. arvense extract caused changes in the structure and hydrogen bonding behavior and composition of the extract proteins. These interactions also caused the extract lipids to accumulate in the insoluble precipitate phase. Most of the phenolics remained in the supernatant phase enhancing the inactivation of trypsin. However, the precipitated compounds were shown to be of apolar in nature as shown in the HPLC chromatograms. Conclusion:The methods that were used showed that the high phenolic content of E. arvense was the main reason for the inhibition of trypsin enzyme activity by denaturing the enzyme. of 1:20. The dry leafs particles were shaked in the solution for overnight at 300 rpm at 24 °C. After the centrifugation at 2000xg for 5 minutes the supernatant was collected into 50 ml falcon tubes. The alcohol in the liquid phase was evaporated with a rotary evaporator. The aqueous extract was frozen for 24 hours and then freeze dried in a lyophilizer (Telstar-Cryodos). Preparation of inhibition solutionE. arvense extract was dissolved in distilled water to a final concentration of 10 mg/ml. By serial dilutions of stock solution 2 mg/ml, 0.2 mg/ml and 0.02 mg/ml concentrations were prepared. Preparation of trypsin solutionBovine pancreatic trypsin was purchased from Fluka Analytical (cat.93610) and used without further purification. Lyophilized powder of bovine pancreatic trypsin (Fluka Analytical, USA) was dissolved in 1 mM HCl to a final concentration of 0.1 mg/ml. Determination of enzyme kineticsTrypsin catalyzes the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE) to N-benzoyl-L-arginine (BA) and ethanol. The slope of the absorbance versus time graph was the production rate of BA at pH 7.6.The reaction was held in a total volume of 3.2 ml quartz cuvette at 25 °C. The unit of trypsin activity was previously determined as 1 µmol BA produced per minute at 253 nm, at pH 7.6 and 25 °C. The reaction was carried out in 100 mM Tris buffer solution. To determine absorption of blank solution, 3050 μl tris buffer and 150 μl of BAEE solution ...

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Synthesis, DNA‐/bovine serum albumin‐binding affinity, and cytotoxicity of dinuclear platinum(II) complexes with 1,6‐naphthyridine‐bridging ligand

Konovalov

Franich

Jurišević

et al. 2020

Applied Organom Chemis

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The dinuclear platinum(II) complexes, [{PtCl(NH 3) 2 } 2 (μ-1,6-nphe)](ClO 4) 2 (Pt1) and [{Pt(en)Cl} 2 (μ-1,6-nphe)](ClO 4) 2 (Pt2) (en is a bidentate-coordinated ethylenediamine and 1,6-nphe is the bridging 1,6-naphthyridine ligand) were synthesized and characterized by different spectroscopic methods. The DNAbinding evaluation of complexes Pt1 and Pt2 was done by UV-Vis, fluorescence emission spectroscopy, and their interaction with bovine serum albumin (BSA). The cytotoxic activity of these complexes was determined against mouse breast (4T1) and colon (CT26) cancer cell lines, human breast (MDA-MB-468), colon (HCT-116), and lung (A549) cancer cell lines as well as mouse mesenchymal stem cells (mMSC). Complex Pt1 showed higher cytotoxic capacity toward solid cancer cell lines compared with Pt2 and lower cytotoxic capacity toward mMSC cells compared with cisplatin. Furthermore, molecular mechanism studies showed that Pt1 complex induced 4T1 and A549 cell apoptosis therefore increasing expression of pro-apoptotic caspase-3 and decreasing expression of anti-apoptotic Bcl-2 and Ki-67. Antitumor capacity of Pt1 complex might be manifested at least in two ways: by facilitating apoptosis and by inhibiting tumor cells proliferation.

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Study of the interaction of kaempferol with bovine serum albumin

Cited by 125 publications

References 25 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

Kinetic and structural characterization of interaction between trypsin and Equisetum arvense extract

Synthesis, DNA‐/bovine serum albumin‐binding affinity, and cytotoxicity of dinuclear platinum(II) complexes with 1,6‐naphthyridine‐bridging ligand

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