Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Wang, Xin; Liu, Yang; He, Lihua; Liu, Bin; Zhang, Siyi; Ye, Xiu; Jing, Jiao-Jiao; Zhang, Jinfeng; Gao, Ming

doi:10.1016/j.fct.2015.01.026

Cited by 67 publications

(29 citation statements)

References 55 publications

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“…It has been reported that the polyphenols of average human dietary intake is about 1g/day, with two-third being flavonoids [27]. In addition, the current reports show that the flavonoids can competitive bind with many drugs and affect their binding affinity to the plasma proteins [10,[28][29][30]. However, to the best of our knowledge, the competitive binding between flavonoids and PMT to the plasma proteins has not been reported.…”

Section: Introductioncontrasting

confidence: 51%

Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

Wang

et al. 2016

Colloids and Surfaces B: Biointerfaces

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Section: Introductioncontrasting

confidence: 51%

Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

Wang

et al. 2016

Colloids and Surfaces B: Biointerfaces

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“…Because of the wide distribution of flavonoids in the human diets, interactions between food components (such as flavonoids) and drugs have recently attracted much attention. Many reports have indicated that flavonoids can change the affinity of drugs for plasma proteins . To our knowledge, the influence of flavonoids on FPZ binding to plasma proteins has still not been investigated.…”

Section: Introductionmentioning

confidence: 99%

Binding of fluphenazine with human serum albumin in the presence of rutin and quercetin: An evaluation of food‐drug interaction by spectroscopic techniques

et al. 2017

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The interactions between human serum albumin (HSA) and fluphenazine (FPZ) in the presence or absence of rutin or quercetin were studied by fluorescence, absorption and circular dichroism (CD) spectroscopy and molecular modeling. The results showed that the fluorescence quenching mechanism was static quenching by the formation of an HSA-FPZ complex. Entropy change (ΔS ) and enthalpy change (ΔH ) values were 68.42 J/(mol⋅K) and -4.637 kJ/mol, respectively, which indicated that hydrophobic interactions and hydrogen bonds played major roles in the acting forces. The interaction process was spontaneous because the Gibbs free energy change (ΔG ) values were negative. The results of competitive experiments demonstrated that FPZ was mainly located within HSA site I (sub-domain IIA). Molecular docking results were in agreement with the experimental conclusions of the thermodynamic parameters and competition experiments. Competitive binding to HSA between flavonoids and FPZ decreased the association constants and increased the binding distances of FPZ binding to HSA. The results of absorption, synchronous fluorescence, three-dimensional fluorescence, and CD spectra showed that the binding of FPZ to HSA caused conformational changes in HSA and simultaneous effects of FPZ and flavonoids induced further HSA conformational changes.

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“…However, reversible attachment of drug to plasma proteins significantly modulates the pharmacodynamics (biological activity and toxicology) and pharmacokinetics (volume of distribution, clearance and elimination half-life) of biologically active compounds [ 29 ]. Hence, studies of interactions between drugs and plasma proteins have an important role in understanding the transport and distribution of drugs in the body, as well as clarifying the mechanism of action, pharmacokinetics and toxicity of drugs [ 31 ].…”

Section: Introductionmentioning

confidence: 99%

The Influence of Glycosylation of Natural and Synthetic Prenylated Flavonoids on Binding to Human Serum Albumin and Inhibition of Cyclooxygenases COX-1 and COX-2

et al. 2017

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The synthesis of different classes of prenylated aglycones (α,β-dihydroxanthohumol (2) and (Z)-6,4’-dihydroxy-4-methoxy-7-prenylaurone (3)) was performed in one step reactions from xanthohumol (1)—major prenylated chalcone naturally occurring in hops. Obtained flavonoids (2–3) and xanthohumol (1) were used as substrates for regioselective fungal glycosylation catalyzed by two Absidia species and Beauveria bassiana. As a result six glycosides (4–9) were formed, of which four glycosides (6–9) have not been published so far. The influence of flavonoid skeleton and the presence of glucopyranose and 4-O-methylglucopyranose moiety in flavonoid molecule on binding to main protein in plasma, human serum albumin (HSA), and inhibition of cyclooxygenases COX-1 and COX-2 were investigated. Results showed that chalcone (1) had the highest binding affinity to HSA (8.624 × 104 M−1) of all tested compounds. It has also exhibited the highest inhibition of cyclooxygenases activity, and it was a two-fold stronger inhibitor than α,β-dihydrochalcone (2) and aurone (3). The presence of sugar moiety in flavonoid molecule caused the loss of HSA binding activity as well as the decrease in inhibition of cyclooxygenases activity.

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Spectroscopic investigation on the food components–drug interaction: The influence of flavonoids on the affinity of nifedipine to human serum albumin

Cited by 67 publications

References 55 publications

Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

Studies on the interaction between promethazine and human serum albumin in the presence of flavonoids by spectroscopic and molecular modeling techniques

Binding of fluphenazine with human serum albumin in the presence of rutin and quercetin: An evaluation of food‐drug interaction by spectroscopic techniques

The Influence of Glycosylation of Natural and Synthetic Prenylated Flavonoids on Binding to Human Serum Albumin and Inhibition of Cyclooxygenases COX-1 and COX-2

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