Amyloid fibrils as dispersing agents for oligothiophenes: control of photophysical properties through nanoscale templating and flow induced fibril alignment
Journal article, 2014

Herein we report that protein fibrils formed from aggregated proteins, so called amyloid fibrils, serve as an excellent dispersing agent for hydrophobic oligothiophenes such as alpha-sexithiophene (6T). Furthermore, the protein fibrils are capable of orienting 6T along the fibril long axis, as demonstrated by flow-aligned linear dichroism spectroscopy and polarized fluorescence microscopy. The materials are prepared by solid state mixing of 6T with a protein capable of self-assembly. This results in a water soluble composite material that upon heating in aqueous acid undergoes self-assembly into protein fibrils non-covalently functionalized with 6T, with a typical diameter of 5-10 nm and lengths in the micrometre range. The resulting aqueous fibril dispersions are a readily available source of oligothiophenes that can be processed from aqueous solvent, and we demonstrate the fabrication of macroscopic structures consisting of aligned 6T functionalized protein fibrils. Due to the fibril induced ordering of 6T these structures exhibit polarized light emission.

LIGHT-EMITTING-DIODES

ELECTRON-MICROSCOPY

BETA-SHEET

DIOXIDE

INSULIN FIBRILS

SILICON

WHITE-LIGHT

ALPHA-OLIGOTHIOPHENES

PROTEIN FIBRILS

INFRARED FTIR SPECTROSCOPY

CONJUGATED POLYMER

Author

F. G. Backlund

Linköping University

Jens Wigenius

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Fredrik Westerlund

Chalmers, Chemical and Biological Engineering, Physical Chemistry

Olle Inganäs

Linköping University

N. Solin

Linköping University

Journal of Materials Chemistry

0959-9428 (ISSN) 1364-5501 (eISSN)

Vol. 2 37 7811-7822

Areas of Advance

Nanoscience and Nanotechnology (2010-2017)

Life Science Engineering (2010-2018)

Subject Categories

Materials Engineering

DOI

10.1039/c4tc00692e

More information

Latest update

2/28/2018