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        <identifier>oai:figshare.com:article/33909229</identifier>
        <datestamp>2026-09-17T19:26:00Z</datestamp>
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        <oai_dc:dc xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance"  xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:dc="http://purl.org/dc/elements/1.1/" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
          <dc:title>Domain Dissolution in Supported Lipid Bilayers Triggered
by Unsaturated Phospholipid Addition</dc:title>
          <dc:creator>Adeyemi
T. Odudimu (25047154)</dc:creator>
          <dc:creator>Nathan J. Wittenberg (1461022)</dc:creator>
          <dc:subject>Biophysics</dc:subject>
          <dc:subject>Biochemistry</dc:subject>
          <dc:subject>Cell Biology</dc:subject>
          <dc:subject>Genetics</dc:subject>
          <dc:subject>Biotechnology</dc:subject>
          <dc:subject>Chemical Sciences not elsewhere classified</dc:subject>
          <dc:subject>Immunology</dc:subject>
          <dc:subject>using fluorescence microscopy</dc:subject>
          <dc:subject>cholera toxin bound</dc:subject>
          <dc:subject>including protein sorting</dc:subject>
          <dc:subject>work also offers</dc:subject>
          <dc:subject>membrane raft ’</dc:subject>
          <dc:subject>since cholesterol stabilizes</dc:subject>
          <dc:subject>dissolving lipid rafts</dc:subject>
          <dc:subject>work describes</dc:subject>
          <dc:subject>redistributing raft</dc:subject>
          <dc:subject>protein profiles</dc:subject>
          <dc:subject>membrane rafts</dc:subject>
          <dc:subject>also known</dc:subject>
          <dc:subject>lipid rafts</dc:subject>
          <dc:subject>membrane microdomains</dc:subject>
          <dc:subject>membrane domain</dc:subject>
          <dc:subject>lipid depletion</dc:subject>
          <dc:subject>lipid content</dc:subject>
          <dc:subject>distinct lipid</dc:subject>
          <dc:subject>surrounding environment</dc:subject>
          <dc:subject>signal transduction</dc:subject>
          <dc:subject>pathogen entry</dc:subject>
          <dc:subject>patches composed</dc:subject>
          <dc:subject>new method</dc:subject>
          <dc:subject>model system</dc:subject>
          <dc:subject>localized molecules</dc:subject>
          <dc:subject>garnered interest</dc:subject>
          <dc:subject>domain dissolution</dc:subject>
          <dc:subject>biophysical factors</dc:subject>
          <dc:subject>biological processes</dc:subject>
          <dc:subject>among others</dc:subject>
          <dc:subject>alternative method</dc:subject>
          <dc:subject>adding liposomes</dc:subject>
          <dc:description>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.</dc:description>
          <dc:date>2026-09-17T00:00:00Z</dc:date>
          <dc:type>Dataset</dc:type>
          <dc:type>Media</dc:type>
          <dc:identifier>10.1021/acs.langmuir.6c03121.s005</dc:identifier>
          <dc:relation>https://figshare.com/articles/media/Domain_Dissolution_in_Supported_Lipid_Bilayers_Triggered_by_Unsaturated_Phospholipid_Addition/33909229</dc:relation>
          <dc:rights>CC BY-NC 4.0</dc:rights>
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