Influence of antioxidant flavonoids quercetin and rutin on the in-vitro binding of neratinib to human serum albumin

Wani, Tanveer A.; Bakheit, Ahmed H.; Zargar, Seema; Alanazi, Zahi Saad; Al-Majed, Abdulhakeem A.

doi:10.1016/j.saa.2020.118977

Cited by 55 publications

(26 citation statements)

References 46 publications

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“…The plasma protein binding is an important parameter in drug pharmacokinetics as the strong or weak binding of drug to plasma protein will ultimately affect the excretion and metabolism of drugs [ [38] , [39] , [40] ]. These effects can thus lead to either toxicity of the drug or may give a sub therapeutic response [ 41 , 42 ]. At higher temperatures the binding stoichiometry decreased as high temperatures increase the disorder of molecules and they vibrate at higher speed.…”

Section: Resultsmentioning

confidence: 99%

“…The synchronous fluorescence technique provides information about the micro-environment of the chromophores present in the protein molecule. The synchronous fluorescence spectroscopy has an advantage of being sensitive, reduced spectral band width and free of several perturbing effects [ 18 , 55 ]. Micro-environmental changes in the Tyr and Trp amino acid residues are suggested if a shift occurs in the emission wavelength.…”

Section: Resultsmentioning

confidence: 99%

“…Conformational changes were also studied with CD since proteins have a certain characteristic far-UV CD spectra (178–250 nm) [ 18 ]. The CD spectra were recorded for the BSA in both the binary and the ternary system.…”

Section: Resultsmentioning

confidence: 99%

“…The plasma protein binding to drugs is necessary to maintain effective therapeutic concertation [ 16 , 17 ]. Displacement of drugs from their binding sites on plasma protein can lead to increased concentration of free drugs in systemic circulation leading to undesired or toxic effects [ [18] , [19] , [20] ]. In this study, in-vitro displacement interaction between azithromycin and colchicine was investigated based on the previous literature where concomitant use of macrolide antibiotics and colchicine resulted in some serious adverse events [ 9 , 10 , 15 ].…”

Section: Introductionmentioning

confidence: 99%

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Binding and drug displacement study of colchicine and bovine serum albumin in presence of azithromycin using multispectroscopic techniques and molecular dynamic simulation

Wani

Bakheit

Al-Majed

et al. 2021

Journal of Molecular Liquids

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The binding and displacement interaction of colchicine and azithromycin to the model transport protein bovine serum albumin (BSA) was evaluated in this study. Azithromycin, a macrolide antibiotic, has antiviral properties and hence, has been used concomitantly with hydroxychloroquine against SARS-CoV-2. Colchicine, a natural plant product is used to treat and prevent acute gout flares. Some macrolide antibiotics are reported to have fatal drug-drug interactions with colchicine. The displacement interaction between colchicine and azithromycin on binding to BSA was evaluated using spectroscopic techniques, molecular docking and molecular dynamic simulation studies. The binding constant recorded for the binary system BSA-colchicine was 7.44 × 10 4 whereas, the binding constant for the ternary system BSA-colchicine in presence of azithromycin was 7.38 × 10 4 and were similar. Azithromycin didn't bind to BSA neither did it interfere in binding of colchicine. The results from molecular docking studies also led to a similar conclusion that azithromycin didn't interfere in the binding of colchicine to BSA. These findings are important since there is possibility of serious adverse event with co-administration of colchicine and azithromycin in patients with underlying gouty arthritis and these patients need to be continuously monitored for colchicine toxicity.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Binding and drug displacement study of colchicine and bovine serum albumin in presence of azithromycin using multispectroscopic techniques and molecular dynamic simulation

Wani

Bakheit

Al-Majed

et al. 2021

Journal of Molecular Liquids

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“…Thermodynamic parameters, such as the Gibb's free energy change (Δ G ), enthalpy change (Δ H ), and entropy change (Δ S ), can help to characterize these interactions. These thermodynamic parameters can be calculated using the van’t Hoff equation as follows (Wani et al., 2021):

\ln K_{a} = ‐ Δ H / R T + Δ S / R

where R is the universal gas constant and T is the temperature, and Δ H and Δ S can be determined from a plot between lnKa versus 1/ T .…”

Section: Resultsmentioning

confidence: 99%

Regulating inhibitory activity of potato I‐type proteinase inhibitor from buckwheat by rutin and quercetin

Cui

Wang

et al. 2021

J Food Biochem

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This study aims to investigate the effects of two flavonoids, rutin and quercetin, on inhibitory activity of recombinant buckwheat trypsin inhibitor (rBTI). We found that rutin and quercetin could quench the florescence of rBTI through the static quenching process. We also observed that upon binding to rutin or quercetin, rBTI underwent conformational changes. The results also suggested that rutin and quercetin bind to two different sites on rBTI through different interactions: rutin binds to rBTI through van der Waals forces and hydrogen bonds, whereas quercetin binds through hydrophobic interactions. Rutin and quercetin also markedly deactivated the trypsin inhibitory activity (TIA) of rBTI, while quercetin exhibited higher inactivation effect on rBTI than rutin due to its structure. Finally, the molecular docking revealed the molecular binding between the flavonoids and rBTI. These findings can be useful for the understanding of how flavonoid affects the inhibitory of rBTI.

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Comparing the interactions of nitrendipine with lysozyme or human serum albumin and the effects of vitamin C and naringin on these interactions by spectroscopy and molecular docking methods

Meng,

Nan,

et al. 2023

Luminescence

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The interactions between drugs and proteins play a pivotal role in determining the pharmacological effects and disposition of drugs within the human body. This study focuses on exploring the interaction between nitrendipine and lysozyme/human serum albumin. Spectroscopic analysis indicated a compound static quenching, indicative of the formation of stable complexes between the drug and proteins. The addition of vitamin C or naringin resulted in a decrease of the binding constant between nitrendipine and lysozyme/human serum albumin. The presence of these compounds may disrupt the interactions between the drug and proteins, potentially leading to an increased concentration of free nitrendipine in the bloodstream. Nitrendipine binds more easily to human serum albumin at 310 K, and human serum albumin has an average binding site ratio with nitrendipine approximately 0.1 higher than that with lysozyme. Vitamin C has a greater impact on the binding constant of nitrendipine to human serum albumin and lysozyme. Compared to the binary system of proteins with the drug, the ternary system with the addition of vitamin C at 310 K reduces the binding constants of lysozyme and human serum albumin by 85%. In conclusion, this study explores the significance of considering drug–protein interactions in understanding drug behavior and potential drug–food interactions.

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Influence of antioxidant flavonoids quercetin and rutin on the in-vitro binding of neratinib to human serum albumin

Cited by 55 publications

References 46 publications

Binding and drug displacement study of colchicine and bovine serum albumin in presence of azithromycin using multispectroscopic techniques and molecular dynamic simulation

Binding and drug displacement study of colchicine and bovine serum albumin in presence of azithromycin using multispectroscopic techniques and molecular dynamic simulation

Regulating inhibitory activity of potato I‐type proteinase inhibitor from buckwheat by rutin and quercetin

Comparing the interactions of nitrendipine with lysozyme or human serum albumin and the effects of vitamin C and naringin on these interactions by spectroscopy and molecular docking methods

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