Characterization of aptamer-protein interactions using optical and acoustic biosensors

Abstract

Optical and acoustic biosensors have been successfully applied in the study of biomolecular interactions for several years. In this thesis, surface plasmon resonance (SPR) spectroscopy, colorimetric assays and quartz crystal microbalance with dissipation monitoring (QCM-D) were employed to characterize the DNA G-quadruplex structure folding as well as the thrombin-aptamer interaction, in combination with different binding schemes (i.e. one step binding, competition and displacement binding, sandwich binding plus a signaling step). All findings in this work would be invaluable in the study of DNA secondary structure and also the DNA-protein interaction on surface, which in consequence will be useful in the development of DNA aptamer-based thrombin biosensors and also establish a model for developing other aptamer-based biosensors and biochips.