GM1 Softens POPC Membranes and Induces the Formation of Micron-Sized Domains.
The influence of the glycolipid GM1 on the physical properties of POPC membranes was studied systematically by using different methods applied to giant and large unilamellar vesicles. The charge per GM1 molecule in the membrane was estimated from electrophoretic mobility measurements. Optical microscopy and differential scanning calorimetry were employed to construct a partial phase diagram of the GM1/POPC system. At room temperature, phase separation in the membrane was detected for GM1 fractions at and above ∼5 mol %, whereby GM1-rich gel-like domains were observed by fluorescent microscopy. Fluctuation analysis, vesicle electrodeformation, and micropipette aspiration were used to assess the bending rigidity of the membrane as a function of GM1 content. In the fluid phase, GM1 was shown to strongly soften the bilayer. In the region of coexistence of fluid and gel-like domains, the micropipette aspiration technique allowed measurements of the bending rigidity of the fluid phase only, whereas electrodeformation and fluctuation analysis were affected by the presence of the gel-phase domains. The observation that GM1 decreased the bilayer bending rigidity is important for understanding the role of this ganglioside in the flexibility of neuronal membranes.
Max Planck Institute of Colloids and Interfaces, Science Park Golm, Potsdam, Germany.
Nico
N
Fricke
Max Planck Institute of Colloids and Interfaces, Science Park Golm, Potsdam, Germany. Electronic address: rumiana.dimova@mpikg.mpg.de.
Rumiana
R
Dimova
D005677:G(M1) Ganglioside / Q000378:metabolism*; D021962:Membrane Microdomains / Q000378:metabolism*; D010713:Phosphatidylcholines / Q000378:metabolism*; D013696:Temperature; D053835:Unilamellar Liposomes / Q000737:chemistry / Q000378:metabolism
D010713:Phosphatidylcholines; D053835:Unilamellar Liposomes; D005677:G(M1) Ganglioside; C028694:1-palmitoyl-2-oleoylphosphatidylcholine