Inhibition of amyloid formation of prion fragment (106–128) by polyphenolic compounds

• Published in: Biochimica et biophysica acta. General subjects Vol. 1869; no. 5; p. 130778
• Main Authors: Regmi, Deepika, Haque, Seymour, Karim, Md Raza Ul, Stanic, Aleksander, Du, Deguo
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2025
• Subjects: Aggregation; amino acids; amyloid; Amyloid - antagonists & inhibitors; Amyloid - chemistry; Amyloid - metabolism; autoxidation; Catechin - analogs & derivatives; Catechin - chemistry; Catechin - pharmacology; catechol; epigallocatechin gallate; flavones; Flavonoid; Humans; Inhibitor; moieties; Peptide Fragments - chemistry; Peptide Fragments - metabolism; peptides; Polyphenol; Polyphenols - chemistry; Polyphenols - pharmacology; Prion; Prion Proteins; prions; Prions - chemistry; Prions - metabolism; Protein Aggregates - drug effects; pyrogallol; quinones; Structure-Activity Relationship; therapeutics; Vicinal hydroxyl; Aggregation; Vicinal hydroxyl; Polyphenol; Prion; Inhibitor; Flavonoid

Prion diseases are characterized by the self-association and amyloid formation of misfolded prion proteins. Developing effective inhibitors of protein aggregation is critical for therapeutic intervention. In this study, we systematically evaluated a range of polyphenolic compounds as potential inhib...