Structures of Aβ17–42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure

• Main Authors: Chebaro, Yassmine, Jiang, Ping, Zang, Tong, Mu, Yuguang, Nguyen, Phuong H., Mousseau, Normand, Derreumaux, Philippe
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2013
• Subjects: DRNTU::Science::Biological sciences
• Online Access: https://hdl.handle.net/10356/99781; http://hdl.handle.net/10220/17181
• Institution: Nanyang Technological University

The amyloid-β protein (Aβ) oligomers are believed to be the main culprits in the cytoxicity of Alzheimer’s disease (AD) and p3 peptides (Aβ17–42 fragments) are present in AD amyloid plaques. Many small-molecule or peptide-based inhibitors are known to slow down Aβ aggregation and reduce the toxicity...