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The interaction of proteins with small molecules is fundamental to theirfunction in living organisms and it is widely studied in drug development. Herewe compare optical trapping dynamics of streptavidin and biotinylatedstreptavidin using a double nanohole optical trap in a metal film. Consistentand clearly distinct behavior is seen between the protein with and without thesmall molecule binding. The real-time dynamics at the single protein level areaccessible with this technique, which also has advantages of not requiringtethering to a surface or the need for exogeneous markers.

Dynamic Variation in Protein-Small Molecule Interaction Observed by Double-Nanohole Optical Trapping