Francesca D’Amico

Research:

I am trained as a medicinal chemist focussed on peptide-based design and synthesis with a strong ambition to combine chemical and biological approaches to apply to drug discovery. Given the importance of ubiquitination cascade in several fundamental biological pathways, I am currently dedicating my research to TRIM (Tripartite Motif) proteins, a large family of RING-type ubiquitin E3 ligases participating in ubiquitin and ubiquitin-like modifications and implicated in certain types of cancers, neurodegenerative disorders and neuromuscular diseases. In order to address TRIM-protein activity, I am working on the development of TRIM targeting options and screening strategies through the design of small molecules or peptide-based inhibitors for further validation in cell-based assays.

Curriculum vitae:

In 2018, I obtained my Master’s degree in Pharmaceutical Chemistry and Technology at the University of Naples Federico II. During my final thesis, I focussed on peptide chemistry, developing N-methylated analogues of therapeutically relevant human peptides acting as GPCR ligands, by using N-methyl scan as a tool to investigate their pharmacological profile. Successively, I moved to Utrecht where I attended an internship in NMR spectroscopy at the Bijvoet Center for Biomolecular research, performing high-resolution studies of antibiotics obtained by recombinant DNA chemistry and molecular biology. In 2019, I joined the Ovaa’s lab as a Marie-Skłodowska-Curie ITN Early Stage Researcher. I’m currently involved in the field of ubiquitin and ubiquitin-like processes as part of the TRIM-NET consortium, working on the design of chemical compounds to modulate TRIM-substrate interactions.