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

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The interaction with gold suppresses fiber-like conformations of the amyloid β (16-22) peptide. / Bellucci, Luca; Ardèvol, Albert; Parrinello, Michele et al.

In: Nanoscale, Vol. 8, No. 16, 2016, p. 8737-48.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Vancouver

Bellucci L, Ardèvol A, Parrinello M, Lutz H, Lu H, Weidner T et al. The interaction with gold suppresses fiber-like conformations of the amyloid β (16-22) peptide. Nanoscale. 2016;8(16):8737-48. doi: 10.1039/c6nr01539e

Author

Bellucci, Luca ; Ardèvol, Albert ; Parrinello, Michele et al. / The interaction with gold suppresses fiber-like conformations of the amyloid β (16-22) peptide. In: Nanoscale. 2016 ; Vol. 8, No. 16. pp. 8737-48.

Bibtex

@article{d93dfe05056a49b099332dcbac8a89c3,

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

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.",

keywords = "Adsorption, Amino Acid Sequence, Amyloid beta-Peptides, Gold, Metal Nanoparticles, Molecular Dynamics Simulation, Nanotechnology, Peptide Fragments, Protein Conformation, Surface Properties, Journal Article, Research Support, Non-U.S. Gov't",

author = "Luca Bellucci and Albert Ard{\`e}vol and Michele Parrinello and Helmut Lutz and Hao Lu and Tobias Weidner and Stefano Corni",

year = "2016",

doi = "10.1039/c6nr01539e",

language = "English",

volume = "8",

pages = "8737--48",

journal = "Nanoscale",

issn = "2040-3364",

publisher = "ROYAL SOC CHEMISTRY",

number = "16",

}

RIS

TY - JOUR

T1 - The interaction with gold suppresses fiber-like conformations of the amyloid β (16-22) peptide

AU - Bellucci, Luca

AU - Ardèvol, Albert

AU - Parrinello, Michele

AU - Lutz, Helmut

AU - Lu, Hao

AU - Weidner, Tobias

AU - Corni, Stefano

PY - 2016

Y1 - 2016

N2 - 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.

AB - 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.

KW - Adsorption

KW - Amino Acid Sequence

KW - Amyloid beta-Peptides

KW - Gold

KW - Metal Nanoparticles

KW - Molecular Dynamics Simulation

KW - Nanotechnology

KW - Peptide Fragments

KW - Protein Conformation

KW - Surface Properties

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1039/c6nr01539e

DO - 10.1039/c6nr01539e

M3 - Journal article

C2 - 27064268

VL - 8

SP - 8737

EP - 8748

JO - Nanoscale

JF - Nanoscale

SN - 2040-3364

IS - 16

ER -