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Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation.

Assarsson, Anna LU ; Linse, Sara LU and Cabaleiro-Lago, Celia LU (2014) In Langmuir 30(29). p.8812-8818
Abstract
The fibril formation of the neurodegenerative peptide amyloid β (Aβ42) is sensitive to solution conditions, and several proteins and peptides have been found to retard the process. Aβ42 fibril formation was followed with ThT fluorescence in the presence of polyamino acids (poly-glutamic acid, poly-lysine, and poly-threonine) and other polymers (poly(acrylic acid), poly(ethylenimine), and poly(diallyldimethylammonium chloride). An accelerating effect on the Aβ42 aggregation process is observed from all positively charged polymers, while no effect is seen from the negative or neutral polymers. The accelerating effect is dependent on the concentration of positive polymer in a highly reproducible manner. Acceleration is observed from a 1:500... (More)
The fibril formation of the neurodegenerative peptide amyloid β (Aβ42) is sensitive to solution conditions, and several proteins and peptides have been found to retard the process. Aβ42 fibril formation was followed with ThT fluorescence in the presence of polyamino acids (poly-glutamic acid, poly-lysine, and poly-threonine) and other polymers (poly(acrylic acid), poly(ethylenimine), and poly(diallyldimethylammonium chloride). An accelerating effect on the Aβ42 aggregation process is observed from all positively charged polymers, while no effect is seen from the negative or neutral polymers. The accelerating effect is dependent on the concentration of positive polymer in a highly reproducible manner. Acceleration is observed from a 1:500 polymer to Aβ42 weight ratio and up. Polyamino acids and the other polymers exert quantitatively the same effect at the same concentrations based on weight. Fibrils are formed in all cases as verified by transmission electron microscopy. The concentrations of polymers required for acceleration are too low to affect the Aβ42 aggregation process through increased ionic strength or molecular crowding effects. Instead, the acceleration seems to arise from the locally increased Aβ42 concentration near the polymers, which favors association and affects the electrostatic environment of the peptide. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
30
issue
29
pages
8812 - 8818
publisher
The American Chemical Society
external identifiers
  • pmid:24978100
  • wos:000339686700022
  • scopus:84904966131
ISSN
0743-7463
DOI
10.1021/la501414j
language
English
LU publication?
yes
id
3a1d6ef6-244b-4146-a71c-0df7e638d15e (old id 4583977)
date added to LUP
2014-09-12 16:43:31
date last changed
2017-08-27 03:29:27
@article{3a1d6ef6-244b-4146-a71c-0df7e638d15e,
  abstract     = {The fibril formation of the neurodegenerative peptide amyloid β (Aβ42) is sensitive to solution conditions, and several proteins and peptides have been found to retard the process. Aβ42 fibril formation was followed with ThT fluorescence in the presence of polyamino acids (poly-glutamic acid, poly-lysine, and poly-threonine) and other polymers (poly(acrylic acid), poly(ethylenimine), and poly(diallyldimethylammonium chloride). An accelerating effect on the Aβ42 aggregation process is observed from all positively charged polymers, while no effect is seen from the negative or neutral polymers. The accelerating effect is dependent on the concentration of positive polymer in a highly reproducible manner. Acceleration is observed from a 1:500 polymer to Aβ42 weight ratio and up. Polyamino acids and the other polymers exert quantitatively the same effect at the same concentrations based on weight. Fibrils are formed in all cases as verified by transmission electron microscopy. The concentrations of polymers required for acceleration are too low to affect the Aβ42 aggregation process through increased ionic strength or molecular crowding effects. Instead, the acceleration seems to arise from the locally increased Aβ42 concentration near the polymers, which favors association and affects the electrostatic environment of the peptide.},
  author       = {Assarsson, Anna and Linse, Sara and Cabaleiro-Lago, Celia},
  issn         = {0743-7463},
  language     = {eng},
  number       = {29},
  pages        = {8812--8818},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation.},
  url          = {http://dx.doi.org/10.1021/la501414j},
  volume       = {30},
  year         = {2014},
}