The use of second harmonic correlation spectroscopy (SHCS) to measure the adsorption and desorption kinetics of proteins to membrane immobilized ligands will be discussed. By measuring the fluctuations of the measured second harmonic (SH) signal, the binding kinetics and thermodynamics of several model protein-ligand binding events on a model membrane surface have ben retrieved through autocorrelation of the measured SH signal. A comparison of the SHCS method with other steady-state equilibrium and kinetic measurements will also be discussed. SHCS has several advantages over existing methods, including a reduction in the amount of analyte required for analysis and faster acquisition times as compared to traditional binding isotherm studies. Additionally, the surface specificity and label-free nature of SHCS eliminate some of the challenges seen in fluorescence correlation spectroscopy. The simplicity and efficiency of SHCS makes it a new and valuable technique to directly and precisely ascertain the binding kinetics of molecules at a surface without a label.

Protein-binding interactions on membranes measured using the new technique of second harmonic correlation spectroscopy

247th National Meeting (2014)

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