Domain Dissolution in Supported Lipid Bilayers Triggered by Unsaturated Phospholipid Addition.
- 1Lehigh University , Department of Chemistry, Bethlehem18015, Pennsylvania, United States.
Abstract
Significant cellular processes, including protein sorting, signal transduction, and pathogen entry, among others, are associated with membrane microdomains, also known as lipid rafts. Lipid rafts, due to their unique biophysical properties compared to their surrounding environment, which stem from their distinct lipid and protein profiles, have garnered interest in methods and techniques that tune their coexisting liquid-ordered/liquid-disordered state, aiming to disrupt or destabilize them. Since cholesterol stabilizes the membrane domain, cholesterol-depleting compounds like cyclodextrin can be used to destabilize and disrupt the membrane rafts. Overall, given the membrane raft's importance in biological processes, it is crucial to understand the biophysical factors that influence its stability. In this study, we present a new method for disrupting and dissolving lipid rafts in a model system of phase-separated supported lipid bilayer (SLB) patches composed of DOPC, DPPC, and cholesterol. Using fluorescence microscopy to monitor the liquid-ordered (Lo) and liquid-disordered (Ld) phases of the SLB patches, we observed that adding DOPC liposomes causes a transformation of the coexisting Ld and Lo phases into a single-phase bilayer. On the other hand, adding liposomes that match the lipid content of the phase-separated SLB patch increases the areas of the existing Ld and Lo phases. This work also offers a new method for redistributing raft-localized molecules, confirmed by tracking the redistribution of cholera toxin bound to GM1 after domain dissolution with DOPC liposomes. The work describes an alternative method for dynamically altering membrane composition and dissolving domains via liposome addition, rather than lipid depletion or exchange.
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BibTeX
@article{odudimu2026domain,
title = {{Domain Dissolution in Supported Lipid Bilayers Triggered by Unsaturated Phospholipid Addition.}},
author = {Adeyemi T Odudimu and Nathan J Wittenberg},
journal = {Langmuir : the ACS journal of surfaces and colloids},
year = {2026},
month = sep,
doi = {10.1021/acs.langmuir.6c03121},
url = {https://europepmc.org/article/MED/42916824},
note = {CC BY},
}
RIS
TY - JOUR
TI - Domain Dissolution in Supported Lipid Bilayers Triggered by Unsaturated Phospholipid Addition.
AU - Adeyemi T Odudimu
AU - Nathan J Wittenberg
PY - 2026
DA - 2026/09/01
JO - Langmuir : the ACS journal of surfaces and colloids
DO - 10.1021/acs.langmuir.6c03121
UR - https://europepmc.org/article/MED/42916824
AB - Significant cellular processes, including protein sorting, signal transduction, and pathogen entry, among others, are associated with membrane microdomains, also known as lipid rafts. Lipid rafts, due to their unique biophysical properties compared to their surrounding environment, which stem from their distinct lipid and protein profiles, have garnered interest in methods and techniques that tune their coexisting liquid-ordered/liquid-disordered state, aiming to disrupt or destabilize them. Since cholesterol stabilizes the membrane domain, cholesterol-depleting compounds like cyclodextrin can be used to destabilize and disrupt the membrane rafts. Overall, given the membrane raft's importance in biological processes, it is crucial to understand the biophysical factors that influence its stability. In this study, we present a new method for disrupting and dissolving lipid rafts in a model system of phase-separated supported lipid bilayer (SLB) patches composed of DOPC, DPPC, and cholesterol. Using fluorescence microscopy to monitor the liquid-ordered (Lo) and liquid-disordered (Ld) phases of the SLB patches, we observed that adding DOPC liposomes causes a transformation of the coexisting Ld and Lo phases into a single-phase bilayer. On the other hand, adding liposomes that match the lipid content of the phase-separated SLB patch increases the areas of the existing Ld and Lo phases. This work also offers a new method for redistributing raft-localized molecules, confirmed by tracking the redistribution of cholera toxin bound to GM1 after domain dissolution with DOPC liposomes. The work describes an alternative method for dynamically altering membrane composition and dissolving domains via liposome addition, rather than lipid depletion or exchange.
SN - 0743-7463
SN - 1520-5827
ER -