Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity

Rikiya Watanabe (), Naoki Soga, Daishi Fujita, Kazuhito V. Tabata, Lisa Yamauchi, Soo Hyeon Kim, Daisuke Asanuma, Mako Kamiya, Yasuteru Urano, Hiroaki Suga () and Hiroyuki Noji ()
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Rikiya Watanabe: Graduate School of Engineering, The University of Tokyo
Naoki Soga: Graduate School of Engineering, The University of Tokyo
Daishi Fujita: Graduate School of Engineering, The University of Tokyo
Kazuhito V. Tabata: Graduate School of Engineering, The University of Tokyo
Lisa Yamauchi: Graduate School of Engineering, The University of Tokyo
Soo Hyeon Kim: CREST, JST
Daisuke Asanuma: Laboratory of Neurobiology, Graduate School of Medicine, The University of Tokyo
Mako Kamiya: Laboratory of Chemical Biology and Molecular Imaging, Graduate School of Medicine, The University of Tokyo
Yasuteru Urano: Laboratory of Chemical Biology and Molecular Imaging, Graduate School of Medicine, The University of Tokyo
Hiroaki Suga: CREST, JST
Hiroyuki Noji: Graduate School of Engineering, The University of Tokyo

Nature Communications, 2014, vol. 5, issue 1, 1-8

Abstract: Abstract Nano- to micron-size reaction chamber arrays (femtolitre chamber arrays) have facilitated the development of sensitive and quantitative biological assays, such as single-molecule enzymatic assays, digital PCR and digital ELISA. However, the versatility of femtolitre chamber arrays is limited to reactions that occur in aqueous solutions. Here we report an arrayed lipid bilayer chamber system (ALBiC) that contains sub-million femtolitre chambers, each sealed with a stable 4-μm-diameter lipid bilayer membrane. When reconstituted with a limiting amount of the membrane transporter proteins α-hemolysin or F0F1-ATP synthase, the chambers within the ALBiC exhibit stochastic and quantized transporting activities. This demonstrates that the single-molecule analysis of passive and active membrane transport is achievable with the ALBiC system. This new platform broadens the versatility of femtolitre chamber arrays and paves the way for novel applications aimed at furthering our mechanistic understanding of membrane proteins’ function.

Date: 2014
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DOI: 10.1038/ncomms5519

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