Publication | Closed Access
Alignment of a Conjugated Polymer onto Amyloid‐like Protein Fibrils
65
Citations
48
References
2007
Year
Insulin FibrilsEngineeringSmart PolymerProtein FoldingPolymer Self-assemblyPolymer ScienceThiophene Acetic AcidBiofabricationAmyloid-like FibrilMacromolecular SystemConjugated PolymerProtein MisfoldingMedicineMacromolecular ArchitectureBiophysicsPolymer ChemistryBiomolecular EngineeringPolymers
The amyloid-like fibril is a biomolecular nanowire template of very high stability. Here we describe the coordination of a conjugated polyelectrolyte, poly(thiophene acetic acid) (PTAA), to bovine insulin fibrils with widths of <10 nm and lengths of up to more than 10 microm. Fibrils complexed with PTAA are aligned on surfaces through molecular combing and transfer printing. Single-molecule spectroscopy techniques are applied to chart spectral variation in the emission of these wires. When these results are combined with analysis of the polarization of the emitted light, we can conclude that the polymer chains are preferentially aligned along the fibrillar axis.
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