Analysis of specific interactions of biomolecules by atomic force microscopy

Abstract

Atomic force microscopy has revealed the potential landscapes of bindings between various biomolecules and ligands. In this review, we introduce previous works that attempted to illustrate the potential landscape of the streptavidin and biotin bond using dynamic force spectroscopy (DFS) and discuss agreements and disagreements with theoretical works. We also introduce our recent work, in which we measured the interaction force at high temporal resolution. Our technique revealed multiple potential minima, which were not observed by DFS. The review also describes the prospective of single-molecule force spectroscopic analysis of biological systems.