The interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide. Issue 16 (11th April 2016)

• Record Type: Journal Article
• Authors: Bellucci, Luca; Ardèvol, Albert; Parrinello, Michele; Lutz, Helmut; Lu, Hao; Weidner, Tobias; Corni, Stefano
• Is Part Of: Nanoscale. Volume 8:Issue 16(2016)
• Page Start: 8737
• Page End: 8748
• Publication Date: 2016-04-11
• Subjects: Nanoscience -- Periodicals; Nanotechnology -- Periodicals; 620.505
• DOI: 10.1039/c6nr01539e
• Languages: English
• ISSNs: 2040-3364

Abstract

Abstract : State-of-the-art classical atomistic molecular dynamics simulations reveal that the interaction of the amyloid β (16–22) peptide with a gold surface is suppressing fiber-like conformations, thanks to the preferential interaction with phenylalanine residues. Abstract : Inorganic surfaces and nanoparticles can accelerate or inhibit the fibrillation process of proteins and peptides, including the biomedically relevant amyloid β peptide. However, the microscopic mechanisms that determine such an effect are still poorly understood. By means of large-scale, state-of-the-art enhanced sampling molecular dynamics simulations, here we identify an interaction mechanism between the segments 16–22 of the amyloid β peptide, known to be fibrillogenic by itself, and the Au(111) surface in water that leads to the suppression of fiber-like conformations from the peptide conformational ensemble. Moreover, thanks to advanced simulation analysis techniques, we characterize the conformational selection vs . induced fit nature of the gold effect. Our results disclose an inhibition mechanism that is rooted in the details of the microscopic peptide–surface interaction rather than in general phenomena such as peptide sequestration from the solution.