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Fibril Charge Affects α-Synuclein Hydrogel Rheological Properties

Pogostin, Brett H. ; Linse, Sara LU and Olsson, Ulf LU (2019) In Langmuir 35(50). p.16536-16544
Abstract

In this paper, we have investigated the interactions between α-synuclein fibrils at different pH values and how this relates to hydrogel formation and gel properties. Using a combination of rheology, small-angle X-ray scattering, Raman spectroscopy, and cryo-transmission electron microscopy (cryo-TEM) experiments, we have been able to investigate the relationship between protein net charge, fibril-fibril interactions, and hydrogel properties, and have explored the potential for α-synuclein to form hydrogels at various conditions. We have found that α-synuclein can form hydrogels at lower concentrations (50-300 μM) and over a wider pH range (6.0-7.5) than previously reported. Over this pH range and at 300 μM, the fibril network is... (More)

In this paper, we have investigated the interactions between α-synuclein fibrils at different pH values and how this relates to hydrogel formation and gel properties. Using a combination of rheology, small-angle X-ray scattering, Raman spectroscopy, and cryo-transmission electron microscopy (cryo-TEM) experiments, we have been able to investigate the relationship between protein net charge, fibril-fibril interactions, and hydrogel properties, and have explored the potential for α-synuclein to form hydrogels at various conditions. We have found that α-synuclein can form hydrogels at lower concentrations (50-300 μM) and over a wider pH range (6.0-7.5) than previously reported. Over this pH range and at 300 μM, the fibril network is electrostatically stabilized. Decreasing the pH to 5.5 results in the precipitation of fibrils. A maximum in gel stiffness was observed at pH 6.5 (∼1300 Pa), which indicates that significant attractive interactions operate at this pH and cause an increase in the density of hydrophobic contacts between the otherwise negatively charged fibrils. We conclude that fibril-fibril interactions under these conditions involve both long-range electrostatic repulsion and a short-range hydrophobic attractive (sticky) component. These results may provide a basis for potential applications and add to the understanding of amyloids.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Langmuir
volume
35
issue
50
pages
9 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:31724872
  • scopus:85076253790
ISSN
0743-7463
DOI
10.1021/acs.langmuir.9b02516
language
English
LU publication?
yes
id
ab9e1154-038c-454f-b46d-c9cbff9294df
date added to LUP
2022-03-29 14:41:58
date last changed
2024-04-24 12:38:36
@article{ab9e1154-038c-454f-b46d-c9cbff9294df,
  abstract     = {{<p>In this paper, we have investigated the interactions between α-synuclein fibrils at different pH values and how this relates to hydrogel formation and gel properties. Using a combination of rheology, small-angle X-ray scattering, Raman spectroscopy, and cryo-transmission electron microscopy (cryo-TEM) experiments, we have been able to investigate the relationship between protein net charge, fibril-fibril interactions, and hydrogel properties, and have explored the potential for α-synuclein to form hydrogels at various conditions. We have found that α-synuclein can form hydrogels at lower concentrations (50-300 μM) and over a wider pH range (6.0-7.5) than previously reported. Over this pH range and at 300 μM, the fibril network is electrostatically stabilized. Decreasing the pH to 5.5 results in the precipitation of fibrils. A maximum in gel stiffness was observed at pH 6.5 (â&amp;circ;¼1300 Pa), which indicates that significant attractive interactions operate at this pH and cause an increase in the density of hydrophobic contacts between the otherwise negatively charged fibrils. We conclude that fibril-fibril interactions under these conditions involve both long-range electrostatic repulsion and a short-range hydrophobic attractive (sticky) component. These results may provide a basis for potential applications and add to the understanding of amyloids.</p>}},
  author       = {{Pogostin, Brett H. and Linse, Sara and Olsson, Ulf}},
  issn         = {{0743-7463}},
  language     = {{eng}},
  number       = {{50}},
  pages        = {{16536--16544}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Langmuir}},
  title        = {{Fibril Charge Affects α-Synuclein Hydrogel Rheological Properties}},
  url          = {{http://dx.doi.org/10.1021/acs.langmuir.9b02516}},
  doi          = {{10.1021/acs.langmuir.9b02516}},
  volume       = {{35}},
  year         = {{2019}},
}