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Multiphoton absorption in amyloid protein fibres

Piotr Hanczyc (Institutionen för kemi- och bioteknik, Fysikalisk kemi) ; M.J. Samoć ; Bengt Nordén (Institutionen för kemi- och bioteknik, Fysikalisk kemi)
Nature Photonics (1749-4885). Vol. 7 (2013), 12, p. 969-972.
[Artikel, refereegranskad vetenskaplig]

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's. Here, we show that amyloids have strong nonlinear optical absorption, which is not present in native non-fibrillized protein. Z-scan 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 mechanism 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.

Nyckelord: NONLINEAR-OPTICAL PROPERTIES, 2-PHOTON ABSORPTION, ORGANOMETALLIC COMPLEXES, COOPERATIVE ENHANCEMENT, FIBRILS, AGGREGATION, DENDRIMER, DISEASE, DNA



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Denna post skapades 2013-11-28. Senast ändrad 2014-04-07.
CPL Pubid: 187774

 

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Institutioner (Chalmers)

Institutionen för kemi- och bioteknik, Fysikalisk kemi (2005-2014)

Ämnesområden

Livsvetenskaper
Materialvetenskap
Nanovetenskap och nanoteknik
Innovation och entreprenörskap (nyttiggörande)
Biofysikalisk kemi
Spektroskopi
Materialkemi
Polymerkemi
Biologisk systematik
Nanoteknik

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