Multiphoton absorption in amyloid protein fibres
Artikel i vetenskaplig tidskrift, 2013

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.

DISEASE

FIBRILS

AGGREGATION

COOPERATIVE ENHANCEMENT

NONLINEAR-OPTICAL PROPERTIES

ORGANOMETALLIC COMPLEXES

DENDRIMER

DNA

2-PHOTON ABSORPTION

Författare

Piotr Hanczyc

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

M.J. Samoć

Bengt Nordén

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

Nature Photonics

1749-4885 (ISSN)

Vol. 7 12 969-972

Ämneskategorier

Polymerkemi

Biologisk systematik

Fysikalisk kemi

Materialkemi

Nanoteknik

Styrkeområden

Nanovetenskap och nanoteknik

Livsvetenskaper och teknik

Materialvetenskap

Fundament

Grundläggande vetenskaper

Drivkrafter

Innovation och entreprenörskap

DOI

10.1038/nphoton.2013.282