Abstract
Fibrillization of peptides leads to the formation of amyloid fibres, which, when in large aggregates, are responsible for diseases such as Alzheimer's and Parkinson's1,2,3,4. Here, we show that amyloids have strong nonlinear optical absorption, which is not present in native non-fibrillized protein. Z-scan5 and pump–probe experiments indicate that insulin and lysozyme β-amyloids, as well as α-synuclein fibres, exhibit either two-photon, three-photon or higher multiphoton absorption processes, depending on the wavelength of light. We propose that the enhanced multiphoton absorption is due to a cooperative mechanism6 involving through-space dipolar coupling between excited states of aromatic amino acids densely packed in the fibrous structures. This finding will provide the opportunity to develop nonlinear optical techniques to detect and study amyloid structures and also suggests that new protein-based materials with sizable multiphoton absorption could be designed for specific applications in nanotechnology, photonics and optoelectronics.
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Acknowledgements
This work was sponsored by a Foundation for Polish Science ‘Welcome’ grant to M.S. and a European Research Council advanced senior grant to B.N.
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P.H. conceived and carried out the experiments. P.H., M.S. and B.N. analysed the results and wrote the manuscript.
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Hanczyc, P., Samoc, M. & Norden, B. Multiphoton absorption in amyloid protein fibres. Nature Photon 7, 969–972 (2013). https://doi.org/10.1038/nphoton.2013.282
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DOI: https://doi.org/10.1038/nphoton.2013.282
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