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      Detection of amyloid fibrils in Parkinson’s disease using plasmonic chirality

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          Abstract

          <p id="d7622878e316">This contribution reports on the application of gold nanorods to the detection of amyloids in Parkinson’s and prion diseases. We found that gold nanorods show no interaction with monomeric proteins but adsorb onto helical protein fibrils. Chiral amyloid templates induce helical arrangement of nanorods, giving rise to intense optical activity at the plasmon resonance wavelengths. This report shows the use of protein fibrils as templates for chiral nanoparticle assembly and development of a biodetection technique. We show this effect on a model recombinant protein, α-synuclein (involved in Parkinson’s disease), using CD, cryogenic transmission EM tomography, and theoretical simulations supporting the experimental findings. We additionally show application to identify patients with Parkinson’s disease from human brain homogenates. </p><p class="first" id="d7622878e319">Amyloid fibrils, which are closely associated with various neurodegenerative 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 α-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. </p>

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          Most cited references36

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          Application of electronic circular dichroism in configurational and conformational analysis of organic compounds.

          This tutorial review is addressed to readers with a background in basic organic chemistry and spectroscopy, but without a specific knowledge of electronic circular dichroism. It describes the fundamental principles, instrumentation, data analysis, and different approaches for interpretation of ECD. The discussion focuses on the application of ECD, also in combination with other methods, in structural analysis of organic compounds, including host-guest complexes, and will emphasize the importance of the interplay between configurational and conformational factors. The tutorial also covers modern supramolecular aspects of ECD and recent developments in computational methods.
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            Is Open Access

            DNA-based Self-Assembly of Chiral Plasmonic Nanostructures with Tailored Optical Response

            Surface plasmon resonances generated in metallic nanostructures can be utilized to tailor electromagnetic fields. The precise spatial arrangement of such structures can result in surprising optical properties that are not found in any naturally occurring material. Here, the designed activity emerges from collective effects of singular components equipped with limited individual functionality. Top-down fabrication of plasmonic materials with a predesigned optical response in the visible range by conventional lithographic methods has remained challenging due to their limited resolution, the complexity of scaling, and the difficulty to extend these techniques to three-dimensional architectures. Molecular self-assembly provides an alternative route to create such materials which is not bound by the above limitations. We demonstrate how the DNA origami method can be used to produce plasmonic materials with a tailored optical response at visible wavelengths. Harnessing the assembly power of 3D DNA origami, we arranged metal nanoparticles with a spatial accuracy of 2 nm into nanoscale helices. The helical structures assemble in solution in a massively parallel fashion and with near quantitative yields. As a designed optical response, we generated giant circular dichroism and optical rotary dispersion in the visible range that originates from the collective plasmon-plasmon interactions within the nanohelices. We also show that the optical response can be tuned through the visible spectrum by changing the composition of the metal nanoparticles. The observed effects are independent of the direction of the incident light and can be switched by design between left- and right-handed orientation. Our work demonstrates the production of complex bulk materials from precisely designed nanoscopic assemblies and highlights the potential of DNA self-assembly for the fabrication of plasmonic nanostructures.
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              Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

              Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.
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                Author and article information

                Journal
                Proceedings of the National Academy of Sciences
                Proc Natl Acad Sci USA
                Proceedings of the National Academy of Sciences
                0027-8424
                1091-6490
                March 27 2018
                March 27 2018
                March 27 2018
                March 12 2018
                : 115
                : 13
                : 3225-3230
                Article
                10.1073/pnas.1721690115
                5879706
                29531058
                cc49c975-b40b-4195-a931-5b2649fd0247
                © 2018

                Free to read

                http://www.pnas.org/site/misc/userlicense.xhtml

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