4.8 Article

Engineering Nanointerfaces of Au25 Clusters for Chaperone-Mediated Peptide Amyloidosis

Journal

NANO LETTERS
Volume 22, Issue 7, Pages 2964-2970

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.2c00149

Keywords

Customizing Nanochaperone; Nanointerface; Gold Nanochaperone; Peptide Amyloidosis

Funding

  1. National Natural Science Foundation of China [21975191, 21805218, 51873168, 22173070]
  2. Natural Science Foundation of Hubei Province [2021CFB299]
  3. Fundamental Research Funds for the Central Universities (WUT) [2021III035JC, 2020III009GX, 2020III035GX]

Ask authors/readers for more resources

By customizing the nanointerfaces of AuNCs, it is possible to precisely manipulate the conformation of peptides, thus controlling their amyloidosis.
Synthetic nanomaterials possessing biomolecular-chaperone functions are good candidates for modulating physicochemical interactions in many bioapplications. Despite extensive research, no general principle to engineer nanomaterial surfaces is available to precisely manipulate biomolecular conformations and behaviors, greatly limiting attempts to develop high-performance nanochaperone materials. Here, we demonstrate that, by quantifying the length (-SCxR +/-, x = 3-11) and charges (R- = -COO-, R+ = -NH3+) of ligands on Au-25 gold nanochaperones (AuNCs), simulating binding sites and affinities of amyloid-like peptides with AuNCs, and probing peptide folding and fibrillation in the presence of AuNCs, it is possible to precisely manipulate the peptides' conformations and, thus, their amyloidosis via customizing AuNCs nanointerfaces. We show that intermediate-length liganded AuNCs with a specific charge chaperone peptides' native conformations and thus inhibit their fibrillation, while other types of AuNCs destabilize peptides and promote their fibrillation. We offer a microscopic molecular insight into peptide identity on AuNCs and provide a guideline in customizing nanochaperones via manipulating their nanointerfaces.

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