ARS | Publication request: Following aptamer-ricin specific binding by single molecule recognition and force spectroscopy measurements

Submitted to: ChemComm
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 30, 2011
Publication Date: January 16, 2012
Citation: Wang, B., Guo, C., Chen, G., Park, B., Xu, B. 2012. Following aptamer-ricin specific binding by single molecule recognition and force spectroscopy measurements. ChemComm. 48:1644-1646.

Interpretive Summary: This research investigated the specific single molecule interactions of food toxin and its probe molecules: antibody and DNA aptamer. Single molecule atomic force microscope (AFM) recognition imaging and dynamic force spectroscopy were used to visualize the interaction and study the interaction dynamics and kinetics. Due to the lack of detailed information of the binding sites, binding affinities of the interactions in the single molecule biophysics/mechano-biochemistry to date, this research provides both sample preparation and AFM tip modification protocols, and the characterization approaches of molecular modeling as well as AFM measurements.

Technical Abstract: The atomic force microscope (AFM) recognition and dynamic force spectroscopy (DFS) experiments provide both morphology and interaction information of the aptamer and protein, which can be used for the future study on the thermodynamics and kinetics properties of ricin-aptamer/antibody interactions. The immobilization method is proved to be able to constrain the ricin conformations on modified Au(111) surface. The molecular simulations provide detailed structural information of the aptamer, antibody and ricin, which are critical when we need understand the functions of these biomolecules and the thermodynamic processes of the binding events. The combination of AFM technique and molecular simulations provide a new approach for the single molecule detection and mechanism study of aptamer.