title: 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.
authors.affiliation: Biomolecular and Organic Electronics, Department of Applied Physics, IFM, Linköping University, Linköping, Sweden. jens.wigenius@chalmers.se
authors.forename: Jens
authors.initials: J
authors.lastname: Wigenius
authors.forename: Gustav
authors.initials: G
authors.lastname: Persson
authors.forename: Jerker
authors.initials: J
authors.lastname: Widengren
authors.forename: Olle
authors.initials: O
authors.lastname: Inganäs
mesh_terms: D000544:Alzheimer Disease / Q000175:diagnosis / Q000473:pathology; D000682:Amyloid / Q000737:chemistry* / Q000378:metabolism; D004573:Electrolytes / Q000737:chemistry; D006801:Humans; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D049449:Luminescence; D008854:Microscopy, Electron; D057139:Nanofibers / Q000032:analysis* / Q000737:chemistry; D036103:Nanotechnology / Q000379:methods*; D011108:Polymers / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D013876:Thiophenes / Q000737:chemistry / Q000378:metabolism
chemical_list: D000682:Amyloid; D004573:Electrolytes; D007328:Insulin; D011108:Polymers; D013876:Thiophenes; C066730:polythiophene