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Complexation of Amyloid Fibrils with Charged Conjugated Polymers

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Title Complexation of Amyloid Fibrils with Charged Conjugated Polymers
 
Creator GHOSH, D
DUTTA, P
CHAKRABORTY, C
SINGH, PK
ANOOP, A
JHA, NN
JACOB, RS
MONDAL, M
MANKAR, S
DAS, S
MALIK, S
MAJI, SK
 
Subject ALPHA-SYNUCLEIN AGGREGATION
PARKINSONS-DISEASE
IN-VITRO
SECONDARY STRUCTURE
ALZHEIMERS-DISEASE
BETA-PROTEIN
TOXICITY
CONFORMATION
MECHANISM
HEPARIN
 
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 a-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.
 
Publisher AMER CHEMICAL SOC
 
Date 2014-12-29T05:55:38Z
2014-12-29T05:55:38Z
2014
 
Type Article
 
Identifier LANGMUIR, 30(13)3775-3786
0743-7463
http://dx.doi.org/10.1021/la404739f
http://dspace.library.iitb.ac.in/jspui/handle/100/17247
 
Language English