SARS-CoV-2 main protease (Mpro) is one of the key enzymes involved in viral replication and transcription by mediating the cleavage maturation events in the precursor polyprotein. With the aim of blocking the Mpro enzyme activity, several new generation of Mpro inhibitors have already been designed but there is still an open need to be tested. As Marche Structural Biology Center (MaSBiC) at Università Politecnica delle Marche (Ancona, Italy), we have the potential of producing high-throughput recombinant Mpro enzyme through bacterial cell factories, with the purpose of testing in-situ new compounds (designed in collaboration with Università di Palermo, Italy) and/or of providing the protein ex-situ for Pharma and Research purposes. Besides the chemical and biological aspects, we offer the possibility of providing advanced biophysical characterizations of Mpro in solution, both on unliganded and bound states, by using neutron techniques (Small Angle Neutron Scattering, SANS, able to determine the monomer – dimer equilibrium and to describe their interface features; Quasi Elastic Neutron Scattering, QENS, providing dynamic information regarding the molecular vibrations), conferring an original and crucial contribution to the development of an effective new drug to fight SARS-CoV-2 coronavirus in COVID-19 outbreak. This unprecedented strategy, accounting for both Mpro monomer-dimer thermodynamic equilibrium and the effect of fast dynamics in drug complexation, will be key for the optimization of the screening procedure of Mpro inhibitors.