Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 115, Issue 13, Pages 3225-3230Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1721690115
Keywords
amyloid; Parkinson's disease; gold nanorods; nanoplasmonics; plasmonic chirality
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Funding
- European Commission under Marie Sklodowska-Curie Program [H2020-MSCA-IF-2015_708321]
- European Research Council [335078, 648071]
- European Commission Grant [EUSMI 731019]
- Spanish Ministry of Economy and Competitiveness (MINECO) [MAT2013-46101-R, AGL2015-65046-C2-1-R, BIO2016-77367-C2-1-R]
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Amyloid fibrils, which are closely associated with various neuro-degenerative diseases, are the final products in many protein aggregation pathways. The identification of fibrils at low concentration is, therefore, pivotal in disease diagnosis and development of therapeutic strategies. We report a methodology for the specific identification of amyloid fibrils using chiroptical effects in plasmonic nanoparticles. The formation of amyloid fibrils based on alpha-synuclein was probed using gold nanorods, which showed no apparent interaction with monomeric proteins but effective adsorption onto fibril structures via noncovalent interactions. The amyloid structure drives a helical nanorod arrangement, resulting in intense optical activity at the surface plasmon resonance wavelengths. This sensing technique was successfully applied to human brain homogenates of patients affected by Parkinson's disease, wherein protein fibrils related to the disease were identified through chiral signals from Au nanorods in the visible and near IR, whereas healthy brain samples did not exhibit any meaningful optical activity. The technique was additionally extended to the specific detection of infectious amyloids formed by prion proteins, thereby confirming the wide potential of the technique. The intense chiral response driven by strong dipolar coupling in helical Au nanorod arrangements allowed us to detect amyloid fibrils down to nanomolar concentrations.
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