Cholesterol accelerates the binding of alzheimer's β-amyloid peptide to ganglioside gm1 through a universal hydrogen-bond-dependent sterol tuning of glycolipid conformation

Frontiers in Physiology

Volumn 4 JUN, Issue , 2013, Pages

  Fantini, Jacques ^a   Yahi, Nouara ^a   Garmy, Nicolas ^a  

^a Aix Marseille University   (France)

Author keywords

Alzheimer; Cholesterol; Ganglioside; Gm1; Langmuir monolayer; Lipid raft; Lipid lipid interaction; Molecular modeling

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[5-16]; CERAMIDE; CHOLESTEROL; DIMER; GANGLIOSIDE GM1; GLYCOLIPID; GLYCONE; HYDROXYL GROUP; PHOSPHATIDYLCHOLINE; SPHINGOMYELIN; STEROL; UNCLASSIFIED DRUG;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; CONFORMATION; CONTROLLED STUDY; GLYCOSIDIC BOND; HYDROGEN BOND; MOLECULAR DYNAMICS; MOLECULAR MODEL; MOLECULAR RECOGNITION; MOLECULAR STABILITY; PHYSICAL CHEMISTRY; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION;

EID: 84884538771     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2013.00120     Document Type: Article

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