Recently the need to design nanoscale, sensitive and flexible bio-sensors or biotic-abiotic interface keeps increasing. One of the essential challenges on this objective is to grasp a thorough understanding of the mechanism governing binding interaction between bio-molecules. In this study we aim to demonstrate the binding specificity and reveal force interaction between the anti-coagulation protein thrombin and the single-stranded DNA thrombin aptamer by application of Atomic Force Microscopy (AFM). The thiolated aptamer was deposited onto gold substrate, and then repeatedly brought into contact with a thrombin-coated AFM tip, and force drop-offs during the pull-off were measured to determine the unbinding force between the thrombin-aptamer pair. The results from experiment show that the thrombin-aptamer pair has specific binding and the force between the pair exhibits loading rate dependence. It was shown that the binding forces of the thrombin-aptamer interaction increases with growth of loading rates. The average binding force for a single thrombin/aptamer pair increased from 20 pN to 40 pN, with loading rate changes from 500pN/s to 13500pN/s. Distribution of the unbinding forces measured for each loading rate can be explained on the basis of single energy barrier model for molecular bond breakage.
- Nanotechnology Institute
- Bioengineering Division
Study on Specific Binding Interaction Between Protein and DNA Aptamer via Dynamic Force Spectroscopy
Ma, X, & Shrotriya, P. "Study on Specific Binding Interaction Between Protein and DNA Aptamer via Dynamic Force Spectroscopy." Proceedings of the ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. ASME 2013 2nd Global Congress on NanoEngineering for Medicine and Biology. Boston, Massachusetts, USA. February 4–6, 2013. V001T06A002. ASME. https://doi.org/10.1115/NEMB2013-93119
Download citation file: