ArticleNature communications2014
Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed.
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- Encapsulated droplet interface bilayers as a platform for high-throughput membrane studies.Soft matter · 2022Article
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- Elucidation and control of low and high active populations of alkaline phosphatase molecules for quantitative digital bioassay.Protein science : a publication of the Protein Society · 2021Article
- Substrate-supported Model Membrane as a Versatile Analytical/Biosensing Platform.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2021Article
Corrections and comments
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Authors and funding
11 authors.
Funding
No grant is acknowledged in the PubMed record.
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.
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