Analyzing the origins of receptor–ligand adhesion forces measured by the scanning force microscope

Abstract

Enthalpic approaches have been shown to be of value in the simulation of scanning force microscope (SFM) force–distance experiments. We show that for streptavidin, adiabatic mapping with lenient minimization convergence criteria can produce useful data for the comparative analysis of different ligands. The lenient mapping protocol profiles the undocking pathway in a fraction of the time required for other methods presented in the literature. Unbinding pathways and hydrogen bonding patterns for three ligands are predicted in a total of 74 computer-hours using a single processor of a Hewlett-Packard J-210. Hence this method allows the analysis of SFM ligand rupture pathways with a low computational overhead and also importantly suggests further avenues of biophysical experimental investigation and data interpretation.