Direct Measurement of Through-Bond Effects in Molecular Multivalent Interactions

Multivalent interactions occur throughout biology, and have a number of characteristics that monovalent interactions do not. However, it remains challenging to directly measure the binding force of molecular multivalent interactions and identify the mechanism of interactions. In this study, the specific interaction between bivalent aptamer and thrombin has been measured directly and quantitatively by force-induced remnant magnetization spectroscopy to investigate the binding force and through-bond effects of the multivalent interactions. The measured differential binding forces enable through-bond effects in thrombin-aptamer complexes to be identified, where aptamer binding at exositeII produces visible effects on their binding at exositeI and vice versa. This method might be suitable for practical applications in the design of high-performance ligands.