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Assessing the interaction between the N-terminal region of the membrane protein magnesium transporter A and a lipid bilayer

Skog, Amanda Eriksson LU ; Jones, Nykola C. ; Månsson, Linda K. LU ; Morth, Jens Preben ; Vrønning Hoffmann, Søren ; Gerelli, Yuri and Skepö, Marie LU orcid (2025) In Journal of Colloid and Interface Science 683. p.663-674
Abstract

This study investigates the interaction of KEIF, the intrinsically disordered N-terminal region of the magnesium transporter MgtA, with lipid bilayers mimicking cell membranes. Combining experimental techniques such as neutron reflectometry (NR), quartz-crystal microbalance with dissipation monitoring (QCM-D), synchrotron radiation circular dichroism (SRCD), and oriented circular dichroism (OCD), with molecular dynamics (MD) simulations, we characterized KEIF's adsorption behavior. Hypothesis: KEIF undergoes conformational changes upon interacting with lipid bilayers, potentially influencing MgtA's function within the plasma membrane. Experiments: The study assessed KEIF's structural transitions and position within lipid bilayers under... (More)

This study investigates the interaction of KEIF, the intrinsically disordered N-terminal region of the magnesium transporter MgtA, with lipid bilayers mimicking cell membranes. Combining experimental techniques such as neutron reflectometry (NR), quartz-crystal microbalance with dissipation monitoring (QCM-D), synchrotron radiation circular dichroism (SRCD), and oriented circular dichroism (OCD), with molecular dynamics (MD) simulations, we characterized KEIF's adsorption behavior. Hypothesis: KEIF undergoes conformational changes upon interacting with lipid bilayers, potentially influencing MgtA's function within the plasma membrane. Experiments: The study assessed KEIF's structural transitions and position within lipid bilayers under various conditions, including zwitterionic versus anionic bilayers and different salt concentrations. The techniques analyzed adsorption-induced structural shifts and peptide localization within the bilayer. Findings: KEIF transitions from a disordered to a more structured state, notably increasing α-helical content upon adsorption to lipid bilayers. The peptide resides primarily in the hydrophobic tail region of the bilayer, where it may displace lipids. Electrostatic interactions, modulated by bilayer charge and ionic strength, play a critical role. These results suggest that KEIF's conformational changes and bilayer interactions can be integral to its potential modulatory role in MgtA function within the plasma membrane. This research highlights the importance of surface-induced structural transitions in intrinsically disordered proteins and their implications for membrane protein modulation.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Intrinsically disordered proteins, Lipid bilayer, MgtA, Peptide adsorption, Protein-lipid interaction
in
Journal of Colloid and Interface Science
volume
683
pages
12 pages
publisher
Academic Press
external identifiers
  • pmid:39706085
  • scopus:85212348434
ISSN
0021-9797
DOI
10.1016/j.jcis.2024.12.064
language
English
LU publication?
yes
id
52d0ddce-90af-4a86-a3ae-86916ac00c74
date added to LUP
2025-02-26 12:02:08
date last changed
2025-07-02 23:04:05
@article{52d0ddce-90af-4a86-a3ae-86916ac00c74,
  abstract     = {{<p>This study investigates the interaction of KEIF, the intrinsically disordered N-terminal region of the magnesium transporter MgtA, with lipid bilayers mimicking cell membranes. Combining experimental techniques such as neutron reflectometry (NR), quartz-crystal microbalance with dissipation monitoring (QCM-D), synchrotron radiation circular dichroism (SRCD), and oriented circular dichroism (OCD), with molecular dynamics (MD) simulations, we characterized KEIF's adsorption behavior. Hypothesis: KEIF undergoes conformational changes upon interacting with lipid bilayers, potentially influencing MgtA's function within the plasma membrane. Experiments: The study assessed KEIF's structural transitions and position within lipid bilayers under various conditions, including zwitterionic versus anionic bilayers and different salt concentrations. The techniques analyzed adsorption-induced structural shifts and peptide localization within the bilayer. Findings: KEIF transitions from a disordered to a more structured state, notably increasing α-helical content upon adsorption to lipid bilayers. The peptide resides primarily in the hydrophobic tail region of the bilayer, where it may displace lipids. Electrostatic interactions, modulated by bilayer charge and ionic strength, play a critical role. These results suggest that KEIF's conformational changes and bilayer interactions can be integral to its potential modulatory role in MgtA function within the plasma membrane. This research highlights the importance of surface-induced structural transitions in intrinsically disordered proteins and their implications for membrane protein modulation.</p>}},
  author       = {{Skog, Amanda Eriksson and Jones, Nykola C. and Månsson, Linda K. and Morth, Jens Preben and Vrønning Hoffmann, Søren and Gerelli, Yuri and Skepö, Marie}},
  issn         = {{0021-9797}},
  keywords     = {{Intrinsically disordered proteins; Lipid bilayer; MgtA; Peptide adsorption; Protein-lipid interaction}},
  language     = {{eng}},
  pages        = {{663--674}},
  publisher    = {{Academic Press}},
  series       = {{Journal of Colloid and Interface Science}},
  title        = {{Assessing the interaction between the N-terminal region of the membrane protein magnesium transporter A and a lipid bilayer}},
  url          = {{http://dx.doi.org/10.1016/j.jcis.2024.12.064}},
  doi          = {{10.1016/j.jcis.2024.12.064}},
  volume       = {{683}},
  year         = {{2025}},
}