Coarse-grained MD simulations reveal beta-amyloid fibrils of various sizes bind to interfacial liquid-ordered and liquid-disordered regions in phase separated lipid rafts with diverse membrane-bound conformational states.

Cheng, Sara Y; Cao, Yiyi; Rouzbehani, Marzieh; Cheng, Kwan H

Cheng, Sara Y; Cao, Yiyi; Rouzbehani, Marzieh; Cheng, Kwan H.

Affiliation

Cheng SY; Department of Physics, University of Texas at Austin, United States.
Cao Y; Department of Neuroscience, Trinity University, United States.
Rouzbehani M; Department of Neuroscience, Trinity University, United States.
Cheng KH; Department of Neuroscience, Trinity University, United States; Department of Physics, Trinity University, United States. Electronic address: kcheng1@trinity.edu.

Biophys Chem ; 260: 106355, 2020 05.

Article in En | MEDLINE | ID: mdl-32179374

Subject(s)

Amyloid beta-Peptides/chemistry; Lipids/chemistry; Molecular Dynamics Simulation; Binding Sites; Humans; Molecular Conformation; Particle Size

Key words

Amyloid fibrils membrane interactions; Coarse-grained model; Lipid rafts; MD simulations; Oxidized cholesterols; Phase-separated lipid domains

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Amyloid beta-Peptides / Molecular Dynamics Simulation / Lipids Limits: Humans Language: En Journal: Biophys Chem Year: 2020 Document type: Article Affiliation country: United States Country of publication: Netherlands

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