Helical sensors of membrane saturation: Changes in orientation and curvature preference
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00143442" target="_blank" >RIV/00216224:14740/25:00143442 - isvavai.cz</a>
Result on the web
<a href="https://www.sciencedirect.com/science/article/pii/S0006349525006228" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0006349525006228</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bpj.2025.09.042" target="_blank" >10.1016/j.bpj.2025.09.042</a>
Alternative languages
Result language
angličtina
Original language name
Helical sensors of membrane saturation: Changes in orientation and curvature preference
Original language description
The degree of unsaturation in lipids, which refers to the number of double bonds in their acyl chains, influences properties such as fluidity and lipid packing. However, it is not well understood how the unsaturation affects the ability of peptides to sense membrane curvature. In our study, we compared membranes with varying levels of unsaturation: monounsaturated POPC; bis-unsaturated DOPC; and polyunsaturated PAPC. We investigated how these membranes interact with peptides of varying hydrophobicity. Using coarse-grained molecular dynamics simulations, we found that increasing unsaturation leads to deeper peptide insertion into the lipid bilayer, which correlates with a shift in curvature preference toward more negative values. We demonstrate that specific peptides preferentially localize on the positively curved regions in saturated membranes but shift preference to negatively curved regions in unsaturated membranes, thereby functioning as sensors of membrane unsaturation. In addition, polyunsaturated lipids facilitate the reorientation of peptides from a membrane-adsorbed state to a transmembrane state. These findings may play a role in biological processes such as vesicle formation, membrane fusion, and protein sorting and highlight the adaptability of peptides to different lipid compositions in membranes.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10610 - Biophysics
Result continuities
Project
<a href="/en/project/LX22NPO5103" target="_blank" >LX22NPO5103: National Institute of Virology and Bacteriology</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
BIOPHYSICAL JOURNAL
ISSN
0006-3495
e-ISSN
1542-0086
Volume of the periodical
124
Issue of the periodical within the volume
23
Country of publishing house
US - UNITED STATES
Number of pages
9
Pages from-to
4087-4095
UT code for WoS article
001634032500001
EID of the result in the Scopus database
2-s2.0-105019810157