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On the micelle formation of DNAJB6b

Carlsson, Andreas LU ; Olsson, Ulf LU and Linse, Sara LU (2023) In QRB Discovery 4.
Abstract

The human chaperone DNAJB6b increases the solubility of proteins involved in protein aggregation diseases and suppresses the nucleation of amyloid structures. Due to such favourable properties, DNAJB6b has gained increasing attention over the past decade. The understanding of how DNAJB6b operates on a molecular level may aid the design of inhibitors against amyloid formation. In this work, fundamental aspects of DNAJB6b self-assembly have been examined, providing a basis for future experimental designs and conclusions. The results imply the formation of large chaperone clusters in a concentration-dependent manner. Microfluidic diffusional sizing (MDS) was used to evaluate how DNAJB6b average hydrodynamic radius varies with... (More)

The human chaperone DNAJB6b increases the solubility of proteins involved in protein aggregation diseases and suppresses the nucleation of amyloid structures. Due to such favourable properties, DNAJB6b has gained increasing attention over the past decade. The understanding of how DNAJB6b operates on a molecular level may aid the design of inhibitors against amyloid formation. In this work, fundamental aspects of DNAJB6b self-assembly have been examined, providing a basis for future experimental designs and conclusions. The results imply the formation of large chaperone clusters in a concentration-dependent manner. Microfluidic diffusional sizing (MDS) was used to evaluate how DNAJB6b average hydrodynamic radius varies with concentration. We found that, in 20 mM sodium phosphate buffer, 0.2 mM EDTA, at pH 8.0 and room temperature, DNAJB6b displays a micellar behaviour, with a critical micelle concentration (CMC) of around 120 nM. The average hydrodynamic radius appears to be concentration independent between ∼10 μM and 100 μM, with a mean radius of about 12 nm. The CMC found by MDS is supported by native agarose gel electrophoresis and the size distribution appears bimodal in the DNAJB6b concentration range ∼100 nM to 4 μM.

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Please use this url to cite or link to this publication:
author
; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
affinity, aggregation, chaperone action, oligomers, self-association
in
QRB Discovery
volume
4
article number
e6
publisher
Cambridge University Press
external identifiers
  • pmid:37593255
  • scopus:85168850937
ISSN
2633-2892
DOI
10.1017/qrd.2023.4
project
Chaperone action - a thermodynamic view
language
English
LU publication?
yes
id
c2a33e72-1612-45e6-b5a7-3403991fea15
date added to LUP
2023-10-30 13:44:55
date last changed
2024-04-19 03:03:13
@article{c2a33e72-1612-45e6-b5a7-3403991fea15,
  abstract     = {{<p>The human chaperone DNAJB6b increases the solubility of proteins involved in protein aggregation diseases and suppresses the nucleation of amyloid structures. Due to such favourable properties, DNAJB6b has gained increasing attention over the past decade. The understanding of how DNAJB6b operates on a molecular level may aid the design of inhibitors against amyloid formation. In this work, fundamental aspects of DNAJB6b self-assembly have been examined, providing a basis for future experimental designs and conclusions. The results imply the formation of large chaperone clusters in a concentration-dependent manner. Microfluidic diffusional sizing (MDS) was used to evaluate how DNAJB6b average hydrodynamic radius varies with concentration. We found that, in 20 mM sodium phosphate buffer, 0.2 mM EDTA, at pH 8.0 and room temperature, DNAJB6b displays a micellar behaviour, with a critical micelle concentration (CMC) of around 120 nM. The average hydrodynamic radius appears to be concentration independent between ∼10 μM and 100 μM, with a mean radius of about 12 nm. The CMC found by MDS is supported by native agarose gel electrophoresis and the size distribution appears bimodal in the DNAJB6b concentration range ∼100 nM to 4 μM.</p>}},
  author       = {{Carlsson, Andreas and Olsson, Ulf and Linse, Sara}},
  issn         = {{2633-2892}},
  keywords     = {{affinity; aggregation; chaperone action; oligomers; self-association}},
  language     = {{eng}},
  publisher    = {{Cambridge University Press}},
  series       = {{QRB Discovery}},
  title        = {{On the micelle formation of DNAJB6b}},
  url          = {{http://dx.doi.org/10.1017/qrd.2023.4}},
  doi          = {{10.1017/qrd.2023.4}},
  volume       = {{4}},
  year         = {{2023}},
}