Presenter Information

Major

Neuroscience

Anticipated Graduation Year

2029

Access Type

Open Access

Abstract

Membrane protein–lipid interactions are critical for cellular signaling but are difficult to study in controlled systems. Here, we synthesized small unilamellar vesicles (SUVs) from DOPC and DOPS lipids using freeze–thaw cycles and extrusion to achieve low polydispersity. SUV size strongly influenced lipid accessibility: highly curved vesicles (<100 nm) introduced packing defects that will enhance lipid transfer to bovine serum albumin (BSA), while larger vesicles show reduced transfer due to tighter packing. DLS and fluorescence measurements support increased stabilization of protein–lipid complexes in smaller SUVs. Differences between DOPC and DOPS further highlight the role of lipid composition in regulating protein–membrane interactions.

Faculty Mentors & Instructors

Dr. Manisha Ray, Assistant professor, Chemistry/Biochemistry : Aryana Sayeed, Graduate Researcher, Chemistry/Biochemistry

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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Biophysical Characterization of Protein-Lipid Interactions Using SUV Model Membranes

Membrane protein–lipid interactions are critical for cellular signaling but are difficult to study in controlled systems. Here, we synthesized small unilamellar vesicles (SUVs) from DOPC and DOPS lipids using freeze–thaw cycles and extrusion to achieve low polydispersity. SUV size strongly influenced lipid accessibility: highly curved vesicles (<100 >nm) introduced packing defects that will enhance lipid transfer to bovine serum albumin (BSA), while larger vesicles show reduced transfer due to tighter packing. DLS and fluorescence measurements support increased stabilization of protein–lipid complexes in smaller SUVs. Differences between DOPC and DOPS further highlight the role of lipid composition in regulating protein–membrane interactions.