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Centre for Misfolding Diseases

Royal Society University Research Fellow

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Dr Pietro Sormanni is a group leader supported by a Royal Society University Research Fellowship. His research focuses on the development of innovative data-driven technologies of rational antibody design, to obtain antibodies against targets that have been challenging to access using conventional approaches, and to improve or predict biophysical properties crucial for the successful development of antibody therapeutics. In his work he has established numerous collaborations and industrial partnerships, whose outcomes are beginning to demonstrate that computational approaches can be applied alongside established procedures to streamline antibody development, and to offer time- and cost-effective novel alternatives.  

Antibodies are key tools to address questions in biomedical research, are widely employed in diagnostics, and are increasingly used as therapeutics to treat many diseases, including cancer and neurodegeneration. Existing methods of antibody discovery and optimisation rely on the laboratory screening of large numbers of variants produced by library construction or by the immune system, which can be time consuming and costly, and sometimes result in antibodies exhibiting sub-optimal properties. Conversely, computational design could drastically reduce time and costs of antibody discovery, and in principle allow for a highly controlled parallel screening of multiple biophysical properties. Moreover, rational design inherently allows targeting specific regions on the target protein (epitopes), which can be particularly daunting using available techniques but is very important for many therapeutic applications.


Prior to taking up this post, Pietro held a postdoctoral Borysiewicz Biomedical Sciences  Fellowship from the University of Cambridge, obtained a PhD in Chemistry from the University of Cambridge, and an MSc in Theoretical Physics from the University of Milan.

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We are always looking for talented and enthusiastic individuals to join the team. If you are interested, please get in touch to discuss potential opportunities.

Selected publications



Dr Sormanni discusses his research

Tour of the Sormanni lab


Automated optimization of the solubility of a hyper-stable α-amylase
M Ali, M Greenig, M Oeller, M Atkinson, X Xu, P Sormanni
– Open Biology
Automated optimisation of the solubility of a hyper-stable α-amylase
M Ali, M Greenig, M Oeller, M Atkinson, X Xu, P Sormanni
– Open Biology
Discovery of potent inhibitors of α-synuclein aggregation using structure-based iterative learning
RI Horne, EA Andrzejewska, P Alam, ZF Brotzakis, A Srivastava, A Aubert, M Nowinska, RC Gregory, R Staats, A Possenti, S Chia, P Sormanni, B Ghetti, B Caughey, TPJ Knowles, M Vendruscolo
– Nature chemical biology
Understanding Biology in the Age of Artificial Intelligence
E Lawrence, A El-Shazly, S Seal, CK Joshi, P Liò, S Singh, A Bender, P Sormanni, M Greenig
Targeted protein editing with an antibody-based system
M Vendruscolo, O Rimon, J Konc, M Ali, VR Chowdhury, P Sormanni, G Bernardes
Improving Antibody Humanness Prediction using Patent Data
T Ucar, A Ramon, D Oglic, R Croasdale-Wood, T Diethe, P Sormanni
Assessing antibody and nanobody nativeness for hit selection and humanization with AbNatiV
A Ramon, M Ali, M Atkinson, A Saturnino, K Didi, C Visentin, S Ricagno, X Xu, M Greenig, P Sormanni
– Nature Machine Intelligence
Sequence-based prediction of the intrinsic solubility of peptides containing non-natural amino acids.
M Oeller, RJD Kang, HL Bolt, AL Gomes Dos Santos, AL Weinmann, A Nikitidis, P Zlatoidsky, W Su, W Czechtizky, L De Maria, P Sormanni, M Vendruscolo
– Nature communications
Score-Based Generative Models for Designing Binding Peptide Backbones
JD Boom, M Greenig, P Sormanni, P Liò
Understanding and controlling the molecular mechanisms of protein aggregation in mAb therapeutics.
KT Pang, YS Yang, W Zhang, YS Ho, P Sormanni, TCT Michaels, I Walsh, S Chia
– Biotechnology Advances
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Group Leader

Research Interest Group

Email address


Clare Hall