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Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces

Tesei, Giulio LU ; Hellstrand, Erik LU ; Sanagavarapu, Kalyani LU ; Linse, Sara LU ; Sparr, Emma LU ; Vácha, Robert and Lund, Mikael LU (2018) In Langmuir 34(4). p.1266-1273
Abstract

Amyloid aggregates are associated with a range of human neurodegenerative disorders, and it has been shown that neurotoxicity is dependent on aggregate size. Combining molecular simulation with analytical theory, a predictive model is proposed for the adsorption of amyloid aggregates onto oppositely charged surfaces, where the interaction is governed by an interplay between electrostatic attraction and entropic repulsion. Predictions are experimentally validated against quartz crystal microbalance-dissipation experiments of amyloid beta peptides and fragmented fibrils in the presence of a supported lipid bilayer. Assuming amyloids as rigid, elongated particles, we observe nonmonotonic trends for the extent of adsorption with respect to... (More)

Amyloid aggregates are associated with a range of human neurodegenerative disorders, and it has been shown that neurotoxicity is dependent on aggregate size. Combining molecular simulation with analytical theory, a predictive model is proposed for the adsorption of amyloid aggregates onto oppositely charged surfaces, where the interaction is governed by an interplay between electrostatic attraction and entropic repulsion. Predictions are experimentally validated against quartz crystal microbalance-dissipation experiments of amyloid beta peptides and fragmented fibrils in the presence of a supported lipid bilayer. Assuming amyloids as rigid, elongated particles, we observe nonmonotonic trends for the extent of adsorption with respect to aggregate size and preferential adsorption of smaller aggregates over larger ones. Our findings describe a general phenomenon with implications for stiff polyions and rodlike particles that are electrostatically attracted to a surface.

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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
34
issue
4
pages
8 pages
publisher
The American Chemical Society
external identifiers
  • scopus:85041447320
ISSN
0743-7463
DOI
10.1021/acs.langmuir.7b03155
language
English
LU publication?
yes
id
e41ce99f-7f0f-44cd-913a-0c8eebd58d69
date added to LUP
2018-02-21 12:41:53
date last changed
2018-05-29 11:43:52
@article{e41ce99f-7f0f-44cd-913a-0c8eebd58d69,
  abstract     = {<p>Amyloid aggregates are associated with a range of human neurodegenerative disorders, and it has been shown that neurotoxicity is dependent on aggregate size. Combining molecular simulation with analytical theory, a predictive model is proposed for the adsorption of amyloid aggregates onto oppositely charged surfaces, where the interaction is governed by an interplay between electrostatic attraction and entropic repulsion. Predictions are experimentally validated against quartz crystal microbalance-dissipation experiments of amyloid beta peptides and fragmented fibrils in the presence of a supported lipid bilayer. Assuming amyloids as rigid, elongated particles, we observe nonmonotonic trends for the extent of adsorption with respect to aggregate size and preferential adsorption of smaller aggregates over larger ones. Our findings describe a general phenomenon with implications for stiff polyions and rodlike particles that are electrostatically attracted to a surface.</p>},
  author       = {Tesei, Giulio and Hellstrand, Erik and Sanagavarapu, Kalyani and Linse, Sara and Sparr, Emma and Vácha, Robert and Lund, Mikael},
  issn         = {0743-7463},
  language     = {eng},
  month        = {01},
  number       = {4},
  pages        = {1266--1273},
  publisher    = {The American Chemical Society},
  series       = {Langmuir},
  title        = {Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces},
  url          = {http://dx.doi.org/10.1021/acs.langmuir.7b03155},
  volume       = {34},
  year         = {2018},
}