Alessio Ciulli

Alessio Ciulli

Company: University of Dundee

Job title: Professor of Chemical Structural Biology


Alessio Ciulli holds the Personal Chair of Structural Chemical Biology at the School of Life Sciences, University of Dundee.

His research interests are on the development of small molecules targeting protein-protein interactions (PPIs) and inducing protein degradation. His group has made significant contributions to selective chemical intervention on important PPI targets. He has pioneered the structure-guided design of drug-like ligands for the von Hippel-Lindau E3 ligase and discovered one of the very first and best characterized bifunctional degrader molecules made of that ligand, the BET PROTAC MZ1. These discoveries helped to realize targeted protein degradation as a revolutionary new modality for therapeutic intervention and have led to significant commercial impact across academia and biopharma worldwide. More recently, Alessio’s Lab has illuminated important structural and mechanistic insights into the molecular recognition and mode of action of degraders, including solving the first crystal structure of a PROTAC ternary complex.

Alessio graduated in Chemistry (University of Florence, 2002) and obtained his PhD in Chemical Biology (University of Cambridge, 2006) studying weak protein-ligand interactions. Following post-doctoral research on fragment-based drug design, and brief HFSP visiting Fellowship at Yale University, he returned to Cambridge in 2009 to start his independent career. In 2013 Alessio moved his laboratory to Dundee and was promoted to Professor in October 2016. He is a Fellow of the Royal Society of Chemistry.


Bringing Proteins Together with Small-Molecule Degraders 9:00 am

Small molecules that recruit proteins to E3 ubiquitin ligases for targeted protein degradation are a novel modality of chemical intervention for biology and medicine Highlighting fundamental structural, biophysical and mechanistic insights into degraders’ ternary complexes, showing that induced protein–protein interaction is a general feature of their molecular recognition Modularity of design, from monovalent glues to…Read more

day: Day One

Discussion/Q&A 10:00 am

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day: Day One

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