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• W2005585708 abstract "Fluorescence assays for ADP detection are of considerable current interest, both in basic research and in drug discovery, as they provide a generic method for measuring the activity of ATPases and kinases. The development of a novel fluorescent biosensor is described that is based on a tetramethylrhodamine-labeled, bacterial actin homologue, ParM. The design of the biosensor takes advantage of the large conformational change of ParM on ADP binding and the strong quenching of the tetramethylrhodamine fluorescence by stacking of the dye. ParM was labeled with two tetramethylrhodamines in close proximity, whereby the fluorophores are able to interact with each other. ADP binding alters the distance and relative orientation of the tetramethylrhodamines, which leads to a change in this stacking interaction and so in the fluorescence intensity. The final ADP biosensor shows ∼15-fold fluorescence increase in response to ADP binding. It has relatively weak affinity for ADP (Kd = 30 μM), enabling it to be used at substoichiometric concentrations relative to ADP, while reporting ADP concentration changes in a wide range around the Kd value, namely, submicromolar to tens of micromolar. The biosensor strongly discriminates against ATP (>100-fold), allowing ADP detection against a background of millimolar ATP. At 20 °C, the labeled ParM binds ADP with a rate constant of 9.5 × 104 M−1 s−1 and the complex dissociates at 2.9 s−1. Thus, the biosensor is suitable for real-time measurements, and its performance in such assays is demonstrated using a sugar kinase and a mammalian protein kinase." @default.
• W2005585708 created "2016-06-24" @default.
• W2005585708 creator A5078281981 @default.
• W2005585708 creator A5087386195 @default.
• W2005585708 date "2010-03-02" @default.
• W2005585708 modified "2023-10-17" @default.
• W2005585708 title "A Fluorescent, Reagentless Biosensor for ADP Based on Tetramethylrhodamine-Labeled ParM" @default.
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• W2005585708 doi "https://doi.org/10.1021/cb9003173" @default.
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