Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

On the self-assembly of αB-crystallin

Lindbladh, Ewelina LU orcid ; Dubackic, Marija LU ; Thacker, Dev LU ; Linse, Sara LU and Olsson, Ulf LU orcid (2025) In Soft Matter 21(37). p.7308-7317
Abstract

The molecular chaperone αB-crystallin is a small heat shock protein that inhibits the aggregation of, among others, Aβ42 and α-synuclein. These proteins are major hallmarks of Alzheimer's and Parkinson's disease, respectively. In order to understand the mechanism with which αB-crystallin performs its chaperone function it is essential to characterize its self-assembly in terms of aggregate size distribution, structure, and critical concentration. The size distribution of the assemblies has been widely discussed and they have been suggested to be monodisperse or polydisperse with varying size distributions covering a range of 10–40 monomers per assembly. Here, the size distribution was studied using dynamic and static light scattering,... (More)

The molecular chaperone αB-crystallin is a small heat shock protein that inhibits the aggregation of, among others, Aβ42 and α-synuclein. These proteins are major hallmarks of Alzheimer's and Parkinson's disease, respectively. In order to understand the mechanism with which αB-crystallin performs its chaperone function it is essential to characterize its self-assembly in terms of aggregate size distribution, structure, and critical concentration. The size distribution of the assemblies has been widely discussed and they have been suggested to be monodisperse or polydisperse with varying size distributions covering a range of 10–40 monomers per assembly. Here, the size distribution was studied using dynamic and static light scattering, microfluidic diffusional sizing (MDS), as well as small-angle X-ray scattering (SAXS). Findings indicate that αB-crystallin has a preference toward forming spherical assemblies consisting of 18 monomers with a hydrodynamic radius of ≈7 nm after one week. SAXS data were modelled using a homogeneous sphere model with a radius of 6 nm, which is comparable to the light scattering and MDS results. 2D classes built from negative stain transmission electron microscopy images suggest that the spherical aggregates contain several smaller globular units. Furthermore, the findings show that the size of the assemblies is independent of protein concentration, supporting a strong preference for specific assembly constellations.

(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
Soft Matter
volume
21
issue
37
pages
10 pages
publisher
Royal Society of Chemistry
external identifiers
  • scopus:105017026329
  • pmid:40891708
ISSN
1744-683X
DOI
10.1039/d5sm00684h
language
English
LU publication?
yes
id
f2bd8f0b-18a1-4d8a-9818-91670001f84e
date added to LUP
2025-11-26 14:27:26
date last changed
2025-11-27 03:00:02
@article{f2bd8f0b-18a1-4d8a-9818-91670001f84e,
  abstract     = {{<p>The molecular chaperone αB-crystallin is a small heat shock protein that inhibits the aggregation of, among others, Aβ42 and α-synuclein. These proteins are major hallmarks of Alzheimer's and Parkinson's disease, respectively. In order to understand the mechanism with which αB-crystallin performs its chaperone function it is essential to characterize its self-assembly in terms of aggregate size distribution, structure, and critical concentration. The size distribution of the assemblies has been widely discussed and they have been suggested to be monodisperse or polydisperse with varying size distributions covering a range of 10–40 monomers per assembly. Here, the size distribution was studied using dynamic and static light scattering, microfluidic diffusional sizing (MDS), as well as small-angle X-ray scattering (SAXS). Findings indicate that αB-crystallin has a preference toward forming spherical assemblies consisting of 18 monomers with a hydrodynamic radius of ≈7 nm after one week. SAXS data were modelled using a homogeneous sphere model with a radius of 6 nm, which is comparable to the light scattering and MDS results. 2D classes built from negative stain transmission electron microscopy images suggest that the spherical aggregates contain several smaller globular units. Furthermore, the findings show that the size of the assemblies is independent of protein concentration, supporting a strong preference for specific assembly constellations.</p>}},
  author       = {{Lindbladh, Ewelina and Dubackic, Marija and Thacker, Dev and Linse, Sara and Olsson, Ulf}},
  issn         = {{1744-683X}},
  language     = {{eng}},
  number       = {{37}},
  pages        = {{7308--7317}},
  publisher    = {{Royal Society of Chemistry}},
  series       = {{Soft Matter}},
  title        = {{On the self-assembly of αB-crystallin}},
  url          = {{http://dx.doi.org/10.1039/d5sm00684h}},
  doi          = {{10.1039/d5sm00684h}},
  volume       = {{21}},
  year         = {{2025}},
}