Cargando…

Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces

[Image: see text] 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 aggregat...

Descripción completa

Detalles Bibliográficos
Autores principales: Tesei, Giulio, Hellstrand, Erik, Sanagavarapu, Kalyani, Linse, Sara, Sparr, Emma, Vácha, Robert, Lund, Mikael
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2017
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5828364/
https://www.ncbi.nlm.nih.gov/pubmed/29284092
http://dx.doi.org/10.1021/acs.langmuir.7b03155
_version_ 1783302628420091904
author Tesei, Giulio
Hellstrand, Erik
Sanagavarapu, Kalyani
Linse, Sara
Sparr, Emma
Vácha, Robert
Lund, Mikael
author_facet Tesei, Giulio
Hellstrand, Erik
Sanagavarapu, Kalyani
Linse, Sara
Sparr, Emma
Vácha, Robert
Lund, Mikael
author_sort Tesei, Giulio
collection PubMed
description [Image: see text] 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.
format Online
Article
Text
id pubmed-5828364
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher American Chemical Society
record_format MEDLINE/PubMed
spelling pubmed-58283642018-02-28 Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces Tesei, Giulio Hellstrand, Erik Sanagavarapu, Kalyani Linse, Sara Sparr, Emma Vácha, Robert Lund, Mikael Langmuir [Image: see text] 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. American Chemical Society 2017-12-28 2018-01-30 /pmc/articles/PMC5828364/ /pubmed/29284092 http://dx.doi.org/10.1021/acs.langmuir.7b03155 Text en Copyright © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Tesei, Giulio
Hellstrand, Erik
Sanagavarapu, Kalyani
Linse, Sara
Sparr, Emma
Vácha, Robert
Lund, Mikael
Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title_full Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title_fullStr Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title_full_unstemmed Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title_short Aggregate Size Dependence of Amyloid Adsorption onto Charged Interfaces
title_sort aggregate size dependence of amyloid adsorption onto charged interfaces
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5828364/
https://www.ncbi.nlm.nih.gov/pubmed/29284092
http://dx.doi.org/10.1021/acs.langmuir.7b03155
work_keys_str_mv AT teseigiulio aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT hellstranderik aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT sanagavarapukalyani aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT linsesara aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT sparremma aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT vacharobert aggregatesizedependenceofamyloidadsorptionontochargedinterfaces
AT lundmikael aggregatesizedependenceofamyloidadsorptionontochargedinterfaces