title: Interactions of polyphenols with plasma proteins: insights from analytical techniques.
abstract: Phenolic compounds are commonly found in natural sources like plant-based foods and beverages. These compounds have received much attention due to their unique biological properties. Polyphenols possess a significant binding affinity for serum albumins which are known to be principal extracellular proteins with a high concentration in blood plasma. They act as carriers of several drugs to different molecular targets. This review summarizes the salient features of the reported work on polyphenol-protein interactions by analytical methods viz., chromatography, circular dichroism, fluorescence spectroscopy (steady state and time resolved), light scattering, equilibrium dialysis, differential scanning calorimetry, UV-vis spectroscopy, isothermal calorimetry, MALDI-TOF mass spectrometry, size exclusion chromatography, capillary electrophoresis, electrospray ionization mass spectrometry, FT-IR, molecular modelling, HPLC, NMR, cyclic voltammetry etc. Polyphenol-serum albumin interaction studies assume significance from the view point of pharmacokinetics and pharmacodynamics.
authors: Department of Chemistry, Karnatak University, Dharwad, India. jseetharam@yahoo.com
authors: Seetharamappa
authors: S
authors: Jaldappagari
authors: Sandhya
authors: S
authors: Balakrishnan
authors: Ashwini H
authors: AH
authors: Hegde
authors: Nagappa L
authors: NL
authors: Teradal
authors: Prashanth S
authors: PS
authors: Narayan
mesh_terms: D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D002623:Chemistry Techniques, Analytical; D006801:Humans; D059808:Polyphenols / Q000494:pharmacology*; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D001798:Blood Proteins; D059808:Polyphenols