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      Thermophoresis in nanoliter droplets to quantify aptamer binding.

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          Abstract

          Biomolecule interactions are central to pharmacology and diagnostics. These interactions can be quantified by thermophoresis, the directed molecule movement along a temperature gradient. It is sensitive to binding induced changes in size, charge, or conformation. Established capillary measurements require at least 0.5 μL per sample. We cut down sample consumption by a factor of 50, using 10 nL droplets produced with acoustic droplet robotics (Labcyte). Droplets were stabilized in an oil-surfactant mix and locally heated with an IR laser. Temperature increase, Marangoni flow, and concentration distribution were analyzed by fluorescence microscopy and numerical simulation. In 10 nL droplets, we quantified AMP-aptamer affinity, cooperativity, and buffer dependence. Miniaturization and the 1536-well plate format make the method high-throughput and automation friendly. This promotes innovative applications for diagnostic assays in human serum or label-free drug discovery screening.

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          Author and article information

          Journal
          Angew. Chem. Int. Ed. Engl.
          Angewandte Chemie (International ed. in English)
          1521-3773
          1433-7851
          Jul 21 2014
          : 53
          : 30
          Affiliations
          [1 ] Systems Biophysics, Physics Department, NanoSystems Initiative Munich and Center for Nanoscience, Ludwig-Maximilians-University Munich, Amalienstrasse 54, 80799 Munich (Germany) http://www.biosystems.physik.lmu.de.
          Article
          10.1002/anie.201402514
          24895233
          © 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

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