Binding and Aggregation Mechanism of Amyloid β‑Peptides onto the GM1 Ganglioside-Containing Lipid Membrane

• Published in: The journal of physical chemistry. B Vol. 117; no. 27; pp. 8085 - 8094
• Main Authors: Hoshino, Tyuji, Mahmood, Md. Iqbal, Mori, Kenichi, Matsuzaki, Katsumi
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 11.07.2013
• Subjects: Agglomeration; Amyloid beta-Peptides - chemistry; Amyloid beta-Peptides - metabolism; Binding; Biological and medical sciences; Computer simulation; Contact; Fundamental and applied biological sciences. Psychology; G(M1) Ganglioside - chemistry; G(M1) Ganglioside - metabolism; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Lipid Bilayers - chemistry; Lipid Bilayers - metabolism; Lipids; Mathematical models; Membranes; Molecular biophysics; Molecular Dynamics Simulation; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Peptides; Protein Binding; Protein Structure, Secondary; Fluctuations; Amyloid; Ganglioside; Adhesion; Molecular cluster; Molecular dynamics method

Accumulation and fibril formation of amyloid β (Aβ) peptides onto a ganglioside-rich lipid membrane is a cause of neuro-disturbance diseases. To find out a measure for suppressing the nucleation of a seed for amyloid fibrils, the mechanism of the initial binding of Aβ to the membrane should be clari...