Atomistic mechanism of polyphenol amyloid aggregation inhibitors: Molecular dynamics study of Curcumin, Exifone, and Myricetin interaction with the segment of tau peptide oligomer

Journal of Biomolecular Structure and Dynamics

Volumn 33, Issue 7, 2015, Pages 1399-1411

  Berhanu, Workalemahu M ^a   Masunov, Artëm E ^a  

^a UNIVERSITY OF CENTRAL FLORIDA   (United States)

Author keywords

aggregation inhibitors; amyloid fibril; binding free energy; Curcumin; Exifone; hydrogen bond; polyphenols; MM PBSA; molecular dynamic simulation; Myricetin

Indexed keywords

AMINO ACID DERIVATIVE; AMYLOID; CURCUMIN; EXIFONE; MYRICETIN; OLIGOMER; TAU PROTEIN; UNCLASSIFIED DRUG; VALYLGLUTAMINYLISOLEUCYLVALYLTYROSYLLYSINE; BENZOPHENONE DERIVATIVE; FLAVONOID; PEPTIDE FRAGMENT; POLYPHENOL; PROTEIN BINDING;

ARTICLE; BETA SHEET; BINDING KINETICS; COVALENT BOND; DRUG MECHANISM; DRUG PROTEIN BINDING; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MODIFICATION; PROTEIN REFOLDING; STATIC ELECTRICITY; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CONFORMATION; DRUG EFFECTS; HUMAN; METABOLISM; PROTEIN MULTIMERIZATION; PROTEINOSIS; QUANTITATIVE STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMYLOID; BENZOPHENONES; CURCUMIN; FLAVONOIDS; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MOLECULAR DYNAMICS SIMULATION; PEPTIDE FRAGMENTS; POLYPHENOLS; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN BINDING; PROTEIN MULTIMERIZATION; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP; TAU PROTEINS;

EID: 84928602022     PISSN: 07391102     EISSN: 15380254     Source Type: Journal    
DOI: 10.1080/07391102.2014.951689     Document Type: Article

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