Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers

Ortigosa-Pascual, Lei LU ; Leiding, Thom LU ; Snogerup-Linse, Sara LU and Pálmadóttir, Tinna LU (2023) In ACS Chemical Neuroscience 14(17). p.3192-3205
Abstract
Photo-induced cross-linking of unmodified proteins (PICUP) has been used in the past to study size distributions of protein assemblies. PICUP may, for example, overcome the significant experimental challenges related to the transient nature, heterogeneity, and low concentration of amyloid protein oligomers relative to monomeric and fibrillar species. In the current study, a reaction chamber was designed, produced, and used for PICUP reaction optimization in terms of reaction conditions and lighting time from ms to s. These efforts make the method more reproducible and accessible and enable the use of shorter reaction times compared to previous studies. We applied the optimized method to an α-synuclein aggregation time course to monitor the... (More)
Photo-induced cross-linking of unmodified proteins (PICUP) has been used in the past to study size distributions of protein assemblies. PICUP may, for example, overcome the significant experimental challenges related to the transient nature, heterogeneity, and low concentration of amyloid protein oligomers relative to monomeric and fibrillar species. In the current study, a reaction chamber was designed, produced, and used for PICUP reaction optimization in terms of reaction conditions and lighting time from ms to s. These efforts make the method more reproducible and accessible and enable the use of shorter reaction times compared to previous studies. We applied the optimized method to an α-synuclein aggregation time course to monitor the relative concentration and size distribution of oligomers over time. The data are compared to the time evolution of the fibril mass concentration, as monitored by thioflavin T fluorescence. At all time points, the smaller the oligomer, the higher its concentration observed after PICUP. Moreover, the total oligomer concentration is highest at short aggregation times, and the decline over time follows the disappearance of monomers. We can therefore conclude that these oligomers form from monomers. (Less)
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
ACS Chemical Neuroscience
volume
14
issue
17
pages
14 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • scopus:85169847670
  • pmid:37621159
ISSN
1948-7193
DOI
10.1021/acschemneuro.3c00326
language
English
LU publication?
yes
id
1777c270-5397-4a3a-9062-217a81617689
date added to LUP
2023-09-15 14:35:48
date last changed
2024-03-16 03:00:20
@article{1777c270-5397-4a3a-9062-217a81617689,
  abstract     = {{Photo-induced cross-linking of unmodified proteins (PICUP) has been used in the past to study size distributions of protein assemblies. PICUP may, for example, overcome the significant experimental challenges related to the transient nature, heterogeneity, and low concentration of amyloid protein oligomers relative to monomeric and fibrillar species. In the current study, a reaction chamber was designed, produced, and used for PICUP reaction optimization in terms of reaction conditions and lighting time from ms to s. These efforts make the method more reproducible and accessible and enable the use of shorter reaction times compared to previous studies. We applied the optimized method to an α-synuclein aggregation time course to monitor the relative concentration and size distribution of oligomers over time. The data are compared to the time evolution of the fibril mass concentration, as monitored by thioflavin T fluorescence. At all time points, the smaller the oligomer, the higher its concentration observed after PICUP. Moreover, the total oligomer concentration is highest at short aggregation times, and the decline over time follows the disappearance of monomers. We can therefore conclude that these oligomers form from monomers.}},
  author       = {{Ortigosa-Pascual, Lei and Leiding, Thom and Snogerup-Linse, Sara and Pálmadóttir, Tinna}},
  issn         = {{1948-7193}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{17}},
  pages        = {{3192--3205}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{ACS Chemical Neuroscience}},
  title        = {{Photo-Induced Cross-Linking of Unmodified α-Synuclein Oligomers}},
  url          = {{http://dx.doi.org/10.1021/acschemneuro.3c00326}},
  doi          = {{10.1021/acschemneuro.3c00326}},
  volume       = {{14}},
  year         = {{2023}},
}