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Article

Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer

1
Electronics-Inspired Interdisciplinary Research Institute, Toyohashi University of Technology, Toyohashi 441-8580, Japan
2
Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan
3
Biosignal Research Center, Kobe University, Kobe 657-8501, Japan
4
Department of Applied Chemistry and Life Science, Toyohashi University of Technology, Toyohashi 441-8580, Japan
*
Authors to whom correspondence should be addressed.
Present Address: Takasaki Advanced Radiation Research Institute, Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology (QST), 1233 Watanuki, Takasaki, Gunma 370-1292, Japan.
Academic Editor: Yosuke Senju
Membranes 2021, 11(5), 339; https://doi.org/10.3390/membranes11050339
Received: 14 April 2021 / Revised: 30 April 2021 / Accepted: 1 May 2021 / Published: 3 May 2021
(This article belongs to the Special Issue Interaction of Proteins with Biomembrane)
We characterized the size, distribution, and fluidity of microdomains in a lipid bilayer containing phosphatidylinositol (PI) and revealed their roles during the two-dimensional assembly of a membrane deformation protein (FBP17). The morphology of the supported lipid bilayer (SLB) consisting of PI and phosphatidylcholine (PC) on a mica substrate was observed with atomic force microscope (AFM). Single particle tracking (SPT) was performed for the PI+PC-SLB on the mica substrate by using the diagonal illumination setup. The AFM topography showed that PI-derived submicron domains existed in the PI+PC-SLB. The spatiotemporal dependence of the lateral lipid diffusion obtained by SPT showed that the microdomain had lower fluidity than the surrounding region and worked as the obstacles for the lipid diffusion. We observed the two-dimensional assembly of FBP17, which is one of F-BAR family proteins included in endocytosis processes and has the function generating lipid bilayer tubules in vitro. At the initial stage of the FBP17 assembly, the PI-derived microdomain worked as a scaffold for the FBP17 adsorption, and the fluid surrounding region supplied FBP17 to grow the FBP17 domain via the lateral molecular diffusion. This study demonstrated an example clearly revealing the roles of two lipid microregions during the protein reaction on a lipid bilayer. View Full-Text
Keywords: lipid bilayer membrane; F-BAR protein; phosphatidylinositol; atomic force microscope; single particle tracking lipid bilayer membrane; F-BAR protein; phosphatidylinositol; atomic force microscope; single particle tracking
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MDPI and ACS Style

Motegi, T.; Takiguchi, K.; Tanaka-Takiguchi, Y.; Itoh, T.; Tero, R. Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer. Membranes 2021, 11, 339. https://doi.org/10.3390/membranes11050339

AMA Style

Motegi T, Takiguchi K, Tanaka-Takiguchi Y, Itoh T, Tero R. Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer. Membranes. 2021; 11(5):339. https://doi.org/10.3390/membranes11050339

Chicago/Turabian Style

Motegi, Toshinori, Kingo Takiguchi, Yohko Tanaka-Takiguchi, Toshiki Itoh, and Ryugo Tero. 2021. "Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer" Membranes 11, no. 5: 339. https://doi.org/10.3390/membranes11050339

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