My main interest is on the X-ray crystallography applications for drug discovery. MX is indeed a valuable tool to determine the structure and function of macromolecules. This method is now widely used by the pharmaceutical industry for the design of new potential candidates. Structural insight gained on a given macromolecular target can lead to the design of new drugs, along with a better comprehension of biological mechanisms.
I also have a keen interest on complementary techniques, such as Small Angle X-ray Scattering (SAXS) and Circular Dichroism (CD), providing additional structural information regarding the macromolecule of interest (for example conformational changes and studies of ligand binding).
At the Unit of Virus and Host-Cell Interactions (UVHCI, UMI 3265 UJF-EMBL-CNRS), I studied the structure and function of part of the replication machinery of the influenza virus, a major human pathogen. Thanks to X-ray crystallography and access to synchrotron facilities, we managed to solve the structure of an important part of the influenza virus polymerase, the endonuclease domain. This new insight on the influenza virus endonuclease, in particular the presence of metallic atoms within the active site, may help to design of new antiviral drugs specific to the influenza virus.
Alexandre Dias joined the Industrial Liaison Office at Diamond in 2011 and is mainly focusing on macromolecular crystallography activities. After a PhD in structural biology at Joseph Fourier University and a Master in management of innovation at Grenoble Business School, he worked within the Business Development team at PX’Therapeutics, in Grenoble, France.
A. Dias, D. Bouvier, T. Crepin, A. A. McCarthy, D.J Hart, F. Baudin, S. Cusack, R.W. Ruigrok, The cap snatching enconuclease of the influenza virus polymerase resides in the PA subunit, Nature (2009), 458 (7240), 914-918.
T. Crepin, A. Dias, A. Palencia, C. Swale, Cusack, R.W. Ruigrok, Mutational and metal binding analysis of the endonuclease domain of the influenza virus polymerase PA subunit. J Virol (2010), 84 (18), 9096-9104.