Journal
NANOSCALE
Volume 8, Issue 16, Pages 8737-8748Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c6nr01539e
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Funding
- MIUR [20105ZZTSE, 2012A7LMS]
- CINECA award under the ISCRA initiative
- European Union [ERC-2009-AdG-247075]
- National Centre of Competence in Research Materials' Revolution: Computational Design and Discovery of Novel Materials (NCCR-MARVEL) project
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Inorganic surfaces and nanoparticles can accelerate or inhibit the fibrillation process of proteins and peptides, including the biomedically relevant amyloid beta 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 beta 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.
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