The interaction with gold suppresses fiber-like conformations of the amyloid β (16-22) peptide

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DOI

  • Luca Bellucci, Università degli Studi di Modena e Reggio Emilia, Centro S3, CNR-NANO Istituto Nanoscienze, Modena, Italy, Italien
  • Albert Ardèvol, ETH, Zurich, Schweiz, USI Università della Svizzera italiana, Schweiz
  • Michele Parrinello, USI Università della Svizzera italiana, ETH, Zurich, Schweiz
  • ,
  • Helmut Lutz, Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany.
  • ,
  • Hao Lu, Max Planck Institute for Polymer Research, Molecular Spectroscopy Department, 55128, Mainz, Germany.
  • ,
  • Tobias Weidner
  • Stefano Corni, Centro S3, CNR-NANO Istituto Nanoscienze, Modena, Italy, USI Università della Svizzera italiana

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.

OriginalsprogEngelsk
TidsskriftNanoscale
Vol/bind8
Nummer16
Sider (fra-til)8737-48
Antal sider12
ISSN2040-3364
DOI
StatusUdgivet - 2016
Eksternt udgivetJa

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