Folding and membrane insertion of amyloid-beta (25-35) peptide and its mutants: Implications for aggregation and neurotoxicity

The mechanisms of interfacial folding and membrane insertion of the Alzheimer's amyloid‐β fragment Aβ(25–35) and its less toxic mutant, N27A‐Aβ(25–35) and more toxic mutant, M35A‐Aβ(25–35), are investigated using replica–exchange molecular dynamics in an implicit water‐membrane environment. Thi...

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Veröffentlicht in:	Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2010-06, Vol.78 (8), p.1909-1925
Hauptverfasser:	Tsai, Hui-Hsu Gavin, Lee, Jian-Bin, Tseng, Sheng-Shiuan, Pan, Xiao-An, Shih, Yuan-Ci
Format:	Artikel
Sprache:	eng
Schlagworte:	aggregation Amyloid beta-Peptides - chemistry Amyloid beta-Peptides - metabolism Amyloid beta-Peptides - toxicity amyloid-beta Cell Membrane - drug effects Cell Membrane - metabolism Humans interfacial folding Magnetic Resonance Spectroscopy membrane insertion Models, Molecular Mutant Proteins - chemistry Mutant Proteins - metabolism Mutant Proteins - toxicity neurotoxicity Neurotoxins - chemistry Neurotoxins - metabolism Neurotoxins - toxicity Peptides - chemistry Peptides - metabolism Peptides - toxicity Protein Folding - drug effects Protein Structure, Quaternary Protein Structure, Secondary Protons replica-exchange molecular dynamics Water - chemistry
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