Impact of the inhibition of proteins activities and the chemical aspect of polyphenols-proteins interactions

• Published in: PharmaNutrition Vol. 7; p. 100142
• Main Authors: Adrar, Nassim Salem, Madani, Khodir, Adrar, Sabah
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.03.2019
• Subjects: alpha-amylase; alpha-glucosidase; amine oxidase (flavin-containing); antioxidants; astringency; atherosclerosis; bioavailability; Chemical aspect; Chemical binding; cholera toxin; coenzyme A; cytochrome P-450; diet; enterotoxins; functional foods; Hepatitis C virus; hepatoprotective effect; hydrogen bonding; hydrophobic bonding; Impact; Inhibition; laminin; leukotoxins; metalloproteinases; microbial enzymes; nutritive value; phospholipase A2; Polyphenol; polyphenols; Protein; public health; RNA-directed DNA polymerase; secondary metabolites; transcription factor NF-kappa B; PRPs; Impact; EGCG; PLA2; CYP3A4; Protein; NF-κB; Polyphenol; Nrf2; LDL; HMG-CoA reductase; Chemical aspect; Keap1; MAO; HCV; Chemical binding; Inhibition; MMP-2 and MMP-9; 67LR

[Display omitted] •Polyphenol-protein interaction depends on the types of protein and polyphenol.•Chemical bindings are primarily hydrophobic interactions and hydrogen bonds.•Astringency may be caused by the polyphenol-protein interactions.•Polyphenols have several very interesting biological activi...