ABSTRACT
The achievement of a complete and unified picture of biorecognition processes in living organisms requires a large effort based on the combination of standard experimental approaches with highly innovative techniques, with the support of adequate theoretical models (see Chapter 1). The traditional concepts of specificity, affinity, and rate constants, widely used to describe biorecognition, have to be updated also to take into account additional aspects, such as the distance and the orientation between the biomolecules, the eventual immobilization on the cell surface, the molecular density, and so on. In this context, single molecule techniques emerged as extremely useful tools to elucidate even subtle details of the biorecognition mechanisms. Dynamic force spectroscopy (DFS) has gained a prominent position among these techniques due to its ability to capture molecular events at the basis of the molecular interaction, well-complementing information coming from standard biomolecular and spectroscopic techniques operating in bulk. This essentially stems from the capability of DFS to measure unbinding forces with picoNewton sensitivity between single couples of biomolecules immobilized on suitable surfaces, under physiological conditions, without labeling and in real time.
