Interaction of phenolic acids and their derivatives with human serum albumin: Structure–affinity relationships and effects on antioxidant activity

Zhang, Yunyue; Wu, Simin; Qin, Yinghui; Liu, Jiaxin; Li, Jingwen; Wang, Qingyu; Ren, Fazheng; Zhang, Hao

doi:10.1016/j.foodchem.2017.07.100

Cited by 53 publications

(22 citation statements)

References 32 publications

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“…Our results show high affinity of 2H4MBA toward HSA (logK = 5.1); however, a recent study suggests a considerably lower stability of 2H4MBA-HSA complex (logK = 3.2) [55]. It may result from the fluorescence emission spectra of 2H4MBA, overlapping with the emission maximum of HSA (Figure 4), disrupting the precise determination of the binding constant in a quenching study (performed Zhang et al) [55]. Previously reported logK values of 3CA-bovine serum albumin (logK = 4.1) [56] and PYR-HSA (logK = 4.5) [18] complexes are in a good agreement with our results.…”

Section: Discussioncontrasting

confidence: 86%

“…HIPA (logK = 3.8), 4-HBA (no interaction), 24DHBA (logK = 3.2), and 34DHBA (logK = 3.1) formed no or poorly stable complexes with HSA [18,[54][55][56], which explains why we did not observe their relevant interactions with albumin in quenching studies. Our results show high affinity of 2H4MBA toward HSA (logK = 5.1); however, a recent study suggests a considerably lower stability of 2H4MBA-HSA complex (logK = 3.2) [55]. It may result from the fluorescence emission spectra of 2H4MBA, overlapping with the emission maximum of HSA (Figure 4), disrupting the precise determination of the binding constant in a quenching study (performed Zhang et al) [55].…”

Section: Discussionmentioning

confidence: 68%

“…The interactions of some compounds tested have been examined in previous studies [18,[53][54][55][56]. The logK value of phenylacetic acid-HSA complex is between 3 and 4 [57,58], and 3M4HPAA (its hydroxy-methoxy-substituted derivative) has a similar affinity toward bovine serum albumin (logK = 3.8) [53].…”

Section: Discussionmentioning

confidence: 99%

“…The logK value of phenylacetic acid-HSA complex is between 3 and 4 [57,58], and 3M4HPAA (its hydroxy-methoxy-substituted derivative) has a similar affinity toward bovine serum albumin (logK = 3.8) [53]. HIPA (logK = 3.8), 4-HBA (no interaction), 24DHBA (logK = 3.2), and 34DHBA (logK = 3.1) formed no or poorly stable complexes with HSA [18,[54][55][56], which explains why we did not observe their relevant interactions with albumin in quenching studies. Our results show high affinity of 2H4MBA toward HSA (logK = 5.1); however, a recent study suggests a considerably lower stability of 2H4MBA-HSA complex (logK = 3.2) [55].…”

Section: Discussionmentioning

confidence: 99%

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Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes

et al. 2020

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Flavonoids are abundant polyphenols in nature. They are extensively biotransformed in enterocytes and hepatocytes, where conjugated (methyl, sulfate, and glucuronide) metabolites are formed. However, bacterial microflora in the human intestines also metabolize flavonoids, resulting in the production of smaller phenolic fragments (e.g., hydroxybenzoic, hydroxyacetic and hydroxycinnamic acids, and hydroxybenzenes). Despite the fact that several colonic metabolites appear in the circulation at high concentrations, we have only limited information regarding their pharmacodynamic effects and pharmacokinetic interactions. Therefore, in this in vitro study, we investigated the interactions of 24 microbial flavonoid metabolites with human serum albumin and cytochrome P450 (CYP2C9, 2C19, and 3A4) enzymes. Our results demonstrated that some metabolites (e.g., 2,4-dihydroxyacetophenone, pyrogallol, O-desmethylangolensin, and 2-hydroxy-4-methoxybenzoic acid) form stable complexes with albumin. However, the compounds tested did not considerably displace Site I and II marker drugs from albumin. All CYP isoforms examined were significantly inhibited by O-desmethylangolensin; nevertheless, only its effect on CYP2C9 seems to be relevant. Furthermore, resorcinol and phloroglucinol showed strong inhibitory effects on CYP3A4. Our results demonstrate that, besides flavonoid aglycones and their conjugated derivatives, some colonic metabolites are also able to interact with proteins involved in the pharmacokinetics of drugs.

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Section: Discussioncontrasting

confidence: 86%

Section: Discussionmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes

et al. 2020

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“…Indeed, association constants of albumin with hydrophobic molecules are, usually, higher than their hydrophilic counterparts. For instance, the methylation of hydroxy groups in phenolic compounds enhanced the binding affinity . Similarly, the increased hydrophobicity due to methoxy groups was demonstrated as a key factor in the affinity with plasmatic proteins .…”

Section: Resultsmentioning

confidence: 99%

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Bertozo

Fernandes

Yoguim

et al. 2020

J of Molecular Recognition

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Fluorescence quenching is widely used to obtain association constants between proteins and ligands. This methodology is based on assumption that ground-state complex between protein and ligand is responsible for quenching. Here, we call the attention about the risk of using the temperature criterion for decision of applying or not fluorescence quenching data to measure association constants. We demonstrated that hydrophobic effect can be the major force involved in the interaction and, as such, superposes the well-established rationalization that host/guest com-

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Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

et al. 2019

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The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF‐HSA interaction were found to fall within the range of 3.79‐5.73 × 104 M˗1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF‐HSA complex, as deduced from the thermodynamic data (ΔS = +133.52 J mol−1 K−1 and ΔH = +13.09 kJ mol−1) of the binding reaction and molecular docking analysis. Three‐dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200‐250 and 250‐300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis.

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Interaction of phenolic acids and their derivatives with human serum albumin: Structure–affinity relationships and effects on antioxidant activity

Cited by 53 publications

References 32 publications

Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes

Testing the Pharmacokinetic Interactions of 24 Colonic Flavonoid Metabolites with Human Serum Albumin and Cytochrome P450 Enzymes

Entropy‐driven binding of octyl gallate in albumin: Failure in the application of temperature effect to distinguish dynamic and static fluorescence quenching

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

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