Abstract
We present a method, Transient Induced Molecular Electronic Spectroscopy (TIMES), to detect protein-ligand interactions without any protein engineering or chemical modification. We developed a physics model for the TIMES signal and mathematically formulated the problem to attain physical insight of protein-ligand interactions without any disturbances by molecular probes, fluorescent labels, or immobilization of molecules. To demonstrate the functionality of this method, we have used the TIMES signals to find the dissociation constants for the affinity of reactions, the shear-stress dependent adsorption time of molecules on surface, and other interesting features of protein-ligand interaction in native conditions. As a unique tool, TIMES offers a simple and effective method to investigate fundamental protein chemistry and drug discoveries.
Highlights
Protein-ligand interaction plays the central role in biomedical process and drug discovery[1,2]
The Transient Induced Molecular Electronic Spectroscopy (TIMES) method measures the signal caused by the dipole moment change when protein and ligand form protein-ligand complex, breaking new grounds for studies of protein-ligand interaction
We report some key characteristics and attractive functions of the TIMES signals, including measurements of reaction dissociation constants between proteins and ligands
Summary
Electronic Spectroscopy (TIMES) for study of protein-ligand interactions received: 14 December 2015 accepted: 03 October 2016 Published: 19 October 2016. The results provide clear evidences that in spite of very similar molecular weight and size of the protein and protein/ligand complex, the binding strength of the two molecules to the electrode show appreciable differences, manifested in the adsorption times measured from the TIMES signals. The above examples demonstrate that from the TIMES signals, one can investigate protein-ligand binding with
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