MODELLING INTERMOLECULAR FORCES IN BIOMOLECULES: FROM PROTEIN-PROTEIN INTERACTIONS TO HALOGEN BONDS.

The accurate description and evaluation of the intermolecular interactions has a great importance in the molecular modelling of biological systems. Protein-protein interactions, in particular, being involved in virtually every cellular process, are nowadays the object of thorough studies aimed at the understanding and modulation of the underlying mechanism. In the Part I of the present work, it will be shown how, through a computational approach, it is possible to get an in-depth analysis of the network of interactions occurring at the interface between tubulin subunits and how vinblastine, a commonly used anticancer agents, is able to interfere with the correct protein association, so having a therapeutic effect. In the Part II, the self-association of the bacterial protein FtsZ will be studied, showing that the detailed description of the protein-protein interactions can provide key information for the de-novo design of inhibiting molecules. Finally, in the Part II, the attention will be focused on the computational study of halogen bonding, which is found to have a great relevance in the recognition process between biological macromolecules and halogenated agents. In particular, it will be shown that a specific approach is mandatory for its correct description in the framework of the classical force-fields.