Biology and Molecular Evolution: Optothermal actuation of fluids and molecules

摘要

We found that the movement of proteins in a temperature gradient is a sensitive and versatile way to probe protein interactions, including the important class of membrane receptors binding to its target molecule. The binding was detected ail-optically in various biological fluids. We screened for drug-protein interactions without labeling the protein and were able to successfully commercialize the method. The physical basis of the movement was studied with DNA and polystyrene beads and could be understood with a capacitor model of ionic shielding.