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

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

  • Bellucci L Dipartimento FIM, Università di Modena e Reggio Emilia, I-41125, Modena, Italy. luca.bellucci_s3@unimore.it and Centro S3, CNR-NANO Istituto Nanoscienze, I-41125, Modena, Italy. stefano.corni@nano.cnr.it.
  • Ardèvol A Department of Chemistry and Applied Biosciences, ETH-Zurich, Switzerland and Facoltà di Informatica, Istituto di Scienze Computazionali, Università della Svizzera Italiana, CH-6900, Lugano, Switzerland.
  • Parrinello M Department of Chemistry and Applied Biosciences, ETH-Zurich, Switzerland and Facoltà di Informatica, Istituto di Scienze Computazionali, Università della Svizzera Italiana, CH-6900, Lugano, Switzerland.
  • Lutz H Max Planck Institute for Polymer Research, D-55128 Mainz, Germany.
  • Lu H Max Planck Institute for Polymer Research, D-55128 Mainz, Germany.
  • Weidner T Max Planck Institute for Polymer Research, D-55128 Mainz, Germany.
  • Corni S Centro S3, CNR-NANO Istituto Nanoscienze, I-41125, Modena, Italy. stefano.corni@nano.cnr.it and Facoltà di Informatica, Istituto di Scienze Computazionali, Università della Svizzera Italiana, CH-6900, Lugano, Switzerland.
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  • 2016-04-12
Published in:
  • Nanoscale. - 2016
Adsorption
Amino Acid Sequence
Amyloid beta-Peptides
Gold
Metal Nanoparticles
Molecular Dynamics Simulation
Nanotechnology
Peptide Fragments
Protein Conformation
Surface Properties
English 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.
Language
  • English
Open access status
hybrid
Identifiers
Persistent URL
https://sonar.ch/global/documents/139963
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