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Characterization of interactions between polyphenolic compounds and human serum proteins by capillary electrophoresis

https://doi.org/10.1007/s00216-008-2046-4

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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High‐throughput capillary electrophoresis frontal analysis method for the study of drug interactions with human serum albumin at near‐physiological conditions

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Determining the binding affinities of phenolic compounds to proteins by quenching of the intrinsic tryptophan fluorescence

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Principles of Therapeutic Drug Monitoring

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Phenolics in ecological interactions: The importance of oxidation

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Investigation of the interaction between flavonoids and human serum albumin

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Comparison of five methods for the study of drug–protein binding in affinity capillary electrophoresis

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Properties of graphical representations of multiple classes of binding sites

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Tannin−Protein Complexes as Radical Scavengers and Radical Sinks

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Interactions between Flavonoids and Proteins: Effect on the Total Antioxidant Capacity

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Polyphenol/Peptide Binding and Precipitation

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Interaction of Flavonoids with Bovine Serum Albumin: A Fluorescence Quenching Study

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Quantitative Examination of Oxidized Polyphenol−Protein Complexes

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Covalent Binding of the Flavonoid Quercetin to Human Serum Albumin

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Phytochemicals: Mechanisms of Action

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Absorption, Bioavailability, and Metabolism of Flavonoids

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Reactions of Plant Phenolics with Food Proteins and Enzymes under Special Consideration of Covalent Bonds

What points at this work

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