“…Herein, MET dimers and the effect of their inhibitors were analyzed from the perspective of stability by atomic force microscopy (AFM) force spectroscopy. AFM can detect the stability, tensile strength, and dissociation kinetics of single molecular bonds with piconewton sensitivity. − What is more, the information provided by AFM force spectroscopy techniques does not require averaging of inhomogeneities, which is very different from block experiments in molecular assemblies. − This provides the potential to assess subtle differences in the stability of the MET dimers. As shown in Scheme A, the MET protein was modified at the tip and substrate, respectively, and in order to maintain the viability and correct conformation of the MET protein, the MET protein was separated from the tip and substrate using a flexible PEG linker and protein A, respectively.…”