Interactions Between a Luminescent Conjugated Oligoelectrolyte and Insulin During Early Phases of Amyloid Formation

Abstract

Aggregates of misfolded proteins play an important role in diseases such as Alzheimer's. Here it is demonstrated how the anionic oligothiophene p-FTAA interacts with and influences pre-fibrillar protein assemblies during the earlier stages of in vitro fibrillation. Conjugated polythiophenes have previously been demonstrated to detect and discriminate between different types of protein aggregates and also introduce luminescent or conductive properties to these nanoscale fiber structures. Fluorescence spectroscopy, DLS, TEM and FCS are employed to follow the interplay between p-FTAA and insulin during in vitro fibrillation. A conjugated oligoelectrolyte (COE) can detect misfolded insulin and influence the kinetics of the early stages of amyloid formation. The growth of structures formed during insulin misfolding is followed by means of light scattering, fluorescence correlation spectroscopy and electron microscopy. A marked influence of the COE on the kinetics of amyloid growth may have relevance for theranostics. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.