I am a researcher currently working in the Computational Structural Biology lab at the University of Utrecht, the Netherlands. Since my PhD, my research interests are in the analysis and prediction of experimental and dynamical data about protein structures and protein interactions. Indeed, proteins are extremely complex objects that carry out the majority of functions in the human body.
Among all the proteins out there, I am deeply fascinated by antibodies and nanobodies: these are immune-derived proteins that are capable of recognizing and neutralizing pathogenic molecules (antigens), binding to a selected region (epitope) on their surface with very high specificity.
These molecules use an intriguing method to recognize their target: basically, antibodies possess six loops whose sequences are adapted and matured to recognize a specific epitope on the antigen. At the genetic level, this is achieved through a process called somatic hypermutation, which introduces random mutations in the immunoglobulin gene to generate a diverse pool of antibodies. The ones that bind the antigen with the highest affinity are then selected and expanded (affinity maturation).
The sequence variability observed in these loops is so high that it is often difficult to predict their structure from the sequence alone, even for state-of-the-art methods such as AlphaFold. Understanding how these proteins recognize and bind their antigen at the structural level is crucial to fine-tune their binding properties and to design new sequences with more desirable features.
To be fair, how cool is this nanobody-antigen complex?
Check out my publications to learn more about my research!