Complexation of Amyloid Fibrils with Charged Conjugated Polymers

It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease as...

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Veröffentlicht in:Langmuir 2014-04, Vol.30 (13), p.3775-3786
Hauptverfasser: Ghosh, Dhiman, Dutta, Paulami, Chakraborty, Chanchal, Singh, Pradeep K, Anoop, A, Jha, Narendra Nath, Jacob, Reeba S, Mondal, Mrityunjoy, Mankar, Shruti, Das, Subhadeep, Malik, Sudip, Maji, Samir K
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container_end_page 3786
container_issue 13
container_start_page 3775
container_title Langmuir
container_volume 30
creator Ghosh, Dhiman
Dutta, Paulami
Chakraborty, Chanchal
Singh, Pradeep K
Anoop, A
Jha, Narendra Nath
Jacob, Reeba S
Mondal, Mrityunjoy
Mankar, Shruti
Das, Subhadeep
Malik, Sudip
Maji, Samir K
description It has been suggested that conjugated charged polymers are amyloid imaging agents and promising therapeutic candidates for neurological disorders. However, very less is known about their efficacy in modulating the amyloid aggregation pathway. Here, we studied the modulation of Parkinson’s disease associated α-synuclein (AS) amyloid assembly kinetics using conjugated polyfluorene polymers (PF, cationic; PFS, anionic). We also explored the complexation of these charged polymers with the various AS aggregated species including amyloid fibrils and oligomers using multidisciplinary biophysical techniques. Our data suggests that both polymers irrespective of their different charges in the side chains increase the fibrilization kinetics of AS and also remarkably change the morphology of the resultant amyloid fibrils. Both polymers were incorporated/aligned onto the AS amyloid fibrils as evident from electron microscopy (EM) and atomic force microscopy (AFM), and the resultant complexes were structurally distinct from their pristine form of both polymers and AS supported by FTIR study. Additionally, we observed that the mechanism of interactions between the polymers with different species of AS aggregates were markedly different.
doi_str_mv 10.1021/la404739f
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subjects alpha-Synuclein - chemistry
alpha-Synuclein - genetics
Amino Acid Sequence
Amyloid - chemistry
Escherichia coli - genetics
Escherichia coli - metabolism
Fluorocarbon Polymers - chemical synthesis
Fluorocarbon Polymers - chemistry
Gene Expression
Humans
Kinetics
Microscopy, Atomic Force
Molecular Sequence Data
Protein Aggregates
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Solutions
Spectroscopy, Fourier Transform Infrared
Static Electricity
Thiazoles
title Complexation of Amyloid Fibrils with Charged Conjugated Polymers
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