The present research features a strong multidisciplinarity, that involves a close integration between organic and medicinal chemistry, pharmacology and computational chemistry disciplines.

The positive outcome of this project is closely related to the extensive use of computational methods as essential tools for the identification of tridimensional structure of ligand-protein complex and for the rational design of specifically tailored small-molecule modulators of the investigated receptors, in order to identify privileged chemical scaffolds able to exert a fine-tuning modulation of GPBAR1 and FXR.

In this context, I am currently involved in performing a series of atomistic simulations and experiments on ligand/receptor binding using the hGPBAR1 homology model and the available rFXR crystal structure.

First, molecular docking calculations will be carried out, representing the fastest way to describe ligand/protein interactions. Then, molecular dynamic (MD) simulations will be performed to identify the major receptor conformational changes responsible for the activity.

In collaboration with my home institution, total synthesis of tailored molecules will be carried out in order to obtain easily synthesizable and more potent compounds in the generation of new therapeutically opportunity in liver and metabolic disorders.