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.

FIBRILS

DENDRIMER

DNA

ORGANOMETALLIC COMPLEXES

2-PHOTON ABSORPTION

DISEASE

NONLINEAR-OPTICAL PROPERTIES

AGGREGATION

COOPERATIVE ENHANCEMENT

Författare

[Person 077d66a7-c35b-445d-a741-b2480f1d8602 not found]

Chalmers, Kemi- och bioteknik, Fysikalisk kemi

[Person 1faadb2a-4e99-407d-b331-4368cd903382 not found]

Politechnika Wrocławska

[Person 1469da0d-0c4c-409e-aae0-928385aaf7f5 not found]

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 (SO 2010-2017, EI 2018-)

Livsvetenskaper och teknik (2010-2018)

Materialvetenskap

Fundament

Grundläggande vetenskaper

Drivkrafter

Innovation och entreprenörskap

DOI

10.1038/nphoton.2013.282

Mer information

Senast uppdaterat

2021-02-17