Templating effect of lipid membranes on Alzheimer's amyloid beta peptide

ChemPhysChem

Volumn 6, Issue 2, 2005, Pages 226-229

  Ege, Canay ^a   Majewski, Jaroslaw ^b   Wu, Guohui ^a   Kjaer, Kristian ^c   Lee, Ka Yee C ^a  

^a UNIVERSITY OF CHICAGO   (United States)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c TECHNICAL UNIVERSITY OF DENMARK   (Denmark)

Author keywords

Alzheimer's disease; Monolayers; Phospholipids; X ray diffraction; X ray reflectivity

Indexed keywords

ASSOCIATION REACTIONS; DYES; GLYCOPROTEINS; MONOLAYERS; NEURODEGENERATIVE DISEASES; PHOSPHOLIPIDS; REFLECTION; X RAY DIFFRACTION;

ALZHEIMER'S DISEASE; AMYLOID-BETA PEPTIDES; GRAZING INCIDENCE X-RAY DIFFRACTION STUDIES; LIPID MEMBRANES; LIPID MONOLAYER; PEPTIDE ASSOCIATION; TEMPLATING EFFECTS; X RAY REFLECTIVITY;

PEPTIDES;

AMYLOID BETA PROTEIN; DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; DIPALMITOYLTRIMETHYLAMMONIOPROPANE; OLIGOMER; TRIMETHYLAMMONIUM SALT DERIVATIVE; UNCLASSIFIED DRUG; 1,2 DIPALMITOYLPHOSPHATIDYLGLYCEROL; 1,2-DIPALMITOYLPHOSPHATIDYLGLYCEROL; CARRIER PROTEIN; LIPID; MEMBRANE LIPID; PEPTIDE; PHOSPHATIDYLGLYCEROL; PHOSPHOLIPID;

ADSORPTION; ALZHEIMER DISEASE; ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; ELECTRIC POTENTIAL; FLUORESCENCE MICROSCOPY; LIPID MEMBRANE; LIPID VESICLE; MEMBRANE DAMAGE; OLIGOMERIZATION; PROTEIN AGGREGATION; PROTEIN DOMAIN; PROTEIN LIPID INTERACTION; PROTEIN LOCALIZATION; SUPRAMOLECULAR CHEMISTRY; SURFACE PROPERTY; X RAY DIFFRACTION; BIOLOGICAL MODEL; BIOPHYSICS; CHEMISTRY; HUMAN; METABOLISM; METHODOLOGY; PHYSICAL CHEMISTRY; PROTEIN CONFORMATION; RADIATION SCATTERING; X RAY;

1,2-DIPALMITOYLPHOSPHATIDYLCHOLINE; ADSORPTION; ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; BIOPHYSICS; CARRIER PROTEINS; CHEMISTRY, PHYSICAL; HUMANS; LIPIDS; MEMBRANE LIPIDS; MODELS, BIOLOGICAL; PEPTIDES; PHOSPHATIDYLGLYCEROLS; PHOSPHOLIPIDS; PROTEIN CONFORMATION; SCATTERING, RADIATION; X-RAYS;

EID: 15044365726     PISSN: 14394235     EISSN: None     Source Type: Journal    
DOI: 10.1002/cphc.200400468     Document Type: Article

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