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Quantification of Membrane Protein Inhibition by Optical Ion Flux in a Droplet Interface Bilayer Array
Author(s) -
Castell Oliver K.,
Berridge James,
Wallace Mark I.
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201107343
Subject(s) - lipid bilayer , total internal reflection fluorescence microscope , membrane , bilayer , interface (matter) , flux (metallurgy) , scalability , chemistry , nanotechnology , computer science , biophysics , materials science , biochemistry , biology , organic chemistry , pulmonary surfactant , gibbs isotherm , database
Optical platforms for assaying membrane protein function offer a promising route to scalable high‐throughput screening (see picture). For the first time quantitative measurements of membrane protein inhibition are reported in an optically addressable lipid bilayer array. Wide‐field total internal reflection fluorescence (TIRF) imaging of Ca 2+ flux enables the quantification of α‐hemolysin inhibition by γ‐cyclodextrin.