Atomic force microscopy and MD simulations reveal pore-like structures of all-d-enantiomer of Alzheimer's β-amyloid peptide: Relevance to the ion channel mechanism of AD pathology

Journal of Physical Chemistry B

Volumn 116, Issue 5, 2012, Pages 1728-1735

  Connelly, Laura ^a   Jang, Hyunbum ^b   Teran Arce, Fernando ^a   Capone, Ricardo ^a   Kotler, Samuel A ^a   Ramachandran, Srinivasan ^a   Kagan, Bruce L ^c   Nussinov, Ruth ^b,d   Lal, Ratnesh ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b SAIC FREDERICK INC   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d TEL AVIV UNIVERSITY   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ATOMIC FORCE MICROSCOPY; CELL MEMBRANES; CHIRALITY; CYTOLOGY; DISEASES; ENANTIOMERS; GLYCOPROTEINS; IONS; LIPID BILAYERS; MEDICAL PROBLEMS; MOLECULAR DYNAMICS; PATHOLOGY; PHYSIOLOGY; THREE DIMENSIONAL;

3D STRUCTURE; AFM; AFM IMAGING; ALZHEIMER; ALZHEIMER'S DISEASE; AMYLOID PEPTIDES; CHANNEL-LIKE STRUCTURES; D-AMINO ACID; DIRECT MECHANISM; ION CHANNEL; IONIC HOMEOSTASIS; L-AMINO ACIDS; L-ENANTIOMERS; LIGAND-RECEPTOR INTERACTIONS; MD SIMULATION; MEMBRANE RECEPTORS; MEMORY LOSS; MOLECULAR DYNAMICS SIMULATIONS; NEURODEGENERATION; PROTEIN MISFOLDING; SENILE PLAQUES; STEREOSPECIFIC;

PEPTIDES;

EID: 84856298593     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp2108126     Document Type: Article

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