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Investigating an asymmetric bilayer as a model of the cytoplasmic leaflet.

Grant number: 24/02663-1
Support Opportunities:Scholarships in Brazil - Master
Effective date (Start): April 01, 2024
Effective date (End): March 31, 2026
Field of knowledge:Physical Sciences and Mathematics - Physics - Condensed Matter Physics
Principal Investigator:Thais Azevedo Enoki Liarte
Grantee:Igor da Silva Oliveira
Host Institution: Instituto de Física (IF). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated research grant:22/04046-4 - Investigating the asymmetry of the plasma membrane: model membranes mimicking healthy and tumor cells, and anti-tumor therapeutic strategies, AP.JP


Formed by hundreds of lipids, proteins, and glycoproteins, cellular membranes represent more than a physical barrier to preserve the internal content from the outside environment. The lipid matrix of cellular membranes comprises various lipids with different chemical structures and physicochemical properties. In particular, the plasma membrane (PM)(eukaryotic) has an exoplasmic leaflet enriched in sphingomyelin (SM), phosphatidylcholine (PC), and cholesterol (chol). In contrast, the inner cytoplasmic leaflet is enriched in phosphatidylethanolamine (PE), phosphatidylserine (PS), and chol. The bilayer asymmetry is essential for cell function. The loss of the bilayer asymmetry is correlated with diseases and apoptosis. Interestingly, two leaflets of different lipid composition, phase behaviors, and order parameters may affect the lipid packing/order of each other. A leaflet with Ld+Lo domains induces an ordered domain across from the genuine Lo phase. Our previous results suggest that these induced ordered domains are enriched in chol. Here, we propose to characterize the induced ordered domains and possibly heterogeneous distribution of PE and PS lipids in a model for this leaflet. In addition, we plan to add phosphatidylinositol 4,5-bisphosphate (PIP2) to the cytoplasmic model leaflet. The characterization of induced ordered domains, possibly with a PIP2 cluster, would have a significant impact on virology. Many reports from virus research conclude that "viruses bud from rafts," though rafts and viral lattice assembly occur on opposite sides of the PM. Upon closer examination, we can resolve the seemingly inconsistent claim by characterizing an induced raft-like domain.

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