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Continuity of Short-Time Dynamics Crossing the Liquid-Liquid Phase Separation in Charge-Tuned Protein Solutions

Mosca, Ilaria ; Beck, Christian ; Jalarvo, Niina H. ; Matsarskaia, Olga ; Roosen-Runge, Felix LU ; Schreiber, Frank and Seydel, Tilo (2024) In Journal of Physical Chemistry Letters 15(48). p.12051-12059
Abstract

Liquid-liquid phase separation (LLPS) constitutes a crucial phenomenon in biological self-organization, not only intervening in the formation of membraneless organelles but also triggering pathological protein aggregation, which is a hallmark in neurodegenerative diseases. Employing incoherent quasi-elastic neutron spectroscopy (QENS), we examine the short-time self-diffusion of a model protein undergoing LLPS as a function of phase splitting and temperature to access information on the nanosecond hydrodynamic response to the cluster formation both within and outside the LLPS regime. We investigate the samples as they dissociate into microdroplets of a dense protein phase dispersed in a dilute phase as well as the separated dense and... (More)

Liquid-liquid phase separation (LLPS) constitutes a crucial phenomenon in biological self-organization, not only intervening in the formation of membraneless organelles but also triggering pathological protein aggregation, which is a hallmark in neurodegenerative diseases. Employing incoherent quasi-elastic neutron spectroscopy (QENS), we examine the short-time self-diffusion of a model protein undergoing LLPS as a function of phase splitting and temperature to access information on the nanosecond hydrodynamic response to the cluster formation both within and outside the LLPS regime. We investigate the samples as they dissociate into microdroplets of a dense protein phase dispersed in a dilute phase as well as the separated dense and dilute phases obtained from centrifugation. By interpreting the QENS results in terms of the local concentrations in the two phases determined by UV-vis spectroscopy, we hypothesize that the short-time transient protein cluster size distribution is conserved at the transition point while the local volume fractions separate.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Physical Chemistry Letters
volume
15
issue
48
pages
9 pages
publisher
The American Chemical Society (ACS)
external identifiers
  • pmid:39589726
  • scopus:85211166661
ISSN
1948-7185
DOI
10.1021/acs.jpclett.4c02533
language
English
LU publication?
yes
id
db533c5a-822b-42b2-a360-b2c5291c9f9e
date added to LUP
2025-01-17 11:14:18
date last changed
2025-07-05 14:44:12
@article{db533c5a-822b-42b2-a360-b2c5291c9f9e,
  abstract     = {{<p>Liquid-liquid phase separation (LLPS) constitutes a crucial phenomenon in biological self-organization, not only intervening in the formation of membraneless organelles but also triggering pathological protein aggregation, which is a hallmark in neurodegenerative diseases. Employing incoherent quasi-elastic neutron spectroscopy (QENS), we examine the short-time self-diffusion of a model protein undergoing LLPS as a function of phase splitting and temperature to access information on the nanosecond hydrodynamic response to the cluster formation both within and outside the LLPS regime. We investigate the samples as they dissociate into microdroplets of a dense protein phase dispersed in a dilute phase as well as the separated dense and dilute phases obtained from centrifugation. By interpreting the QENS results in terms of the local concentrations in the two phases determined by UV-vis spectroscopy, we hypothesize that the short-time transient protein cluster size distribution is conserved at the transition point while the local volume fractions separate.</p>}},
  author       = {{Mosca, Ilaria and Beck, Christian and Jalarvo, Niina H. and Matsarskaia, Olga and Roosen-Runge, Felix and Schreiber, Frank and Seydel, Tilo}},
  issn         = {{1948-7185}},
  language     = {{eng}},
  number       = {{48}},
  pages        = {{12051--12059}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Physical Chemistry Letters}},
  title        = {{Continuity of Short-Time Dynamics Crossing the Liquid-Liquid Phase Separation in Charge-Tuned Protein Solutions}},
  url          = {{http://dx.doi.org/10.1021/acs.jpclett.4c02533}},
  doi          = {{10.1021/acs.jpclett.4c02533}},
  volume       = {{15}},
  year         = {{2024}},
}