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• W2130658655 abstract "Membrane-protein interaction plays key roles in a wide variety of biological processes. Although various methods have been employed to measure membrane binding of soluble proteins, a robust high-throughput assay that is universally applicable to all proteins is lacking at present. Here we report a new fluorescence quenching assay utilizing enhanced green fluorescence protein (EGFP)-fusion proteins and a lipid containing a dark quencher, N-dimethylaminoazobenzenesulfonyl-phosphatidylethanolamine (dabsyl-PE). The EGFP fluorescence emission intensity showed a large decrease (i.e., >50%) when EGFP-fusion proteins bound the vesicles containing 5 mol% dabsyl-PE. This simple assay, which can be performed using either a cuvette-based spectrofluorometer or a fluorescence plate reader, allowed rapid, sensitive, and accurate determination of lipid specificity and affinity for various lipid binding domains, including two pleckstrin homology domains, an epsin N-terminal homology domain, and a phox homology domain. The assay can also be applied to high-throughput screening of small molecules that modulate membrane binding of proteins." @default.
• W2130658655 created "2016-06-24" @default.
• W2130658655 creator A5018265320 @default.
• W2130658655 creator A5026339029 @default.
• W2130658655 creator A5051546853 @default.
• W2130658655 date "2013-12-01" @default.
• W2130658655 modified "2023-10-01" @default.
• W2130658655 title "High-throughput fluorescence assay for membrane-protein interaction" @default.
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• W2130658655 doi "https://doi.org/10.1194/jlr.d041376" @default.
• W2130658655 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3826699" @default.
• W2130658655 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24006510" @default.
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