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Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation
[Image: see text] 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-glu...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4191606/ https://www.ncbi.nlm.nih.gov/pubmed/24978100 http://dx.doi.org/10.1021/la501414j |
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author | Assarsson, Anna Linse, Sara Cabaleiro-Lago, Celia |
author_facet | Assarsson, Anna Linse, Sara Cabaleiro-Lago, Celia |
author_sort | Assarsson, Anna |
collection | PubMed |
description | [Image: see text] 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. |
format | Online Article Text |
id | pubmed-4191606 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-41916062014-10-09 Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation Assarsson, Anna Linse, Sara Cabaleiro-Lago, Celia Langmuir [Image: see text] 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. American Chemical Society 2014-06-30 2014-07-29 /pmc/articles/PMC4191606/ /pubmed/24978100 http://dx.doi.org/10.1021/la501414j Text en Copyright © 2014 American Chemical Society Terms of Use (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) |
spellingShingle | Assarsson, Anna Linse, Sara Cabaleiro-Lago, Celia Effects of Polyamino Acids and Polyelectrolytes on Amyloid β Fibril Formation |
title | Effects of Polyamino Acids and Polyelectrolytes on
Amyloid β Fibril Formation |
title_full | Effects of Polyamino Acids and Polyelectrolytes on
Amyloid β Fibril Formation |
title_fullStr | Effects of Polyamino Acids and Polyelectrolytes on
Amyloid β Fibril Formation |
title_full_unstemmed | Effects of Polyamino Acids and Polyelectrolytes on
Amyloid β Fibril Formation |
title_short | Effects of Polyamino Acids and Polyelectrolytes on
Amyloid β Fibril Formation |
title_sort | effects of polyamino acids and polyelectrolytes on
amyloid β fibril formation |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4191606/ https://www.ncbi.nlm.nih.gov/pubmed/24978100 http://dx.doi.org/10.1021/la501414j |
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