Royal Society University Research Fellow

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Research

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.

Background

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.

Join our group

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.

 

Watch Dr Sormanni give a seminar on the group's research (April 2025).

 

 

Dr Sormanni discusses his research

Tour of the Sormanni lab

Publications

Systematic Activity Maturation of a Single-Domain Antibody with Non-canonical Amino Acids through Chemical Mutagenesis.
PR Lindstedt, FA Aprile, P Sormanni, R Rakoto, CM Dobson, GJL Bernardes, M Vendruscolo
Cell chemical biology
(2020)
28
Pairs of amino acids at the P- and A-sites of the ribosome predictably and causally modulate translation-elongation rates.
N Ahmed, UA Friedrich, P Sormanni, P Ciryam, NS Altman, B Bukau, G Kramer, EP O'Brien
Journal of molecular biology
(2020)
432
A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease
T Ikenoue, FA Aprile, P Sormanni, FS Ruggeri, M Perni, GT Heller, CP Haas, C Middel, R Limbocker, B Mannini, TCT Michaels, TPJ Knowles, CM Dobson, M Vendruscolo
Scientific Reports
(2020)
10
Rationally designed antibodies as research tools to study the > structure-toxicity relationship of amyloid-b oligomers
R Limbocker, B Mannini, R Cataldi, S Chhangur, AK Wright, RP Kreiser, JA Albright, S Chia, J Habchi, P Sormanni, JR Kumita, FS Ruggeri, CM Dobson, F Chiti, FA Aprile, M Vendruscolo
International Journal of Molecular Sciences
(2020)
21
Rational design of a conformation-specific antibody for the quantification of Aβ oligomers
FA Aprile, P Sormanni, M Podpolny, S Chhangur, L-M Needham, FS Ruggeri, M Perni, R Limbocker, GT Heller, T Sneideris, T Scheidt, B Mannini, J Habchi, SF Lee, PC Salinas, TPJ Knowles, CM Dobson, M Vendruscolo
Proceedings of the National Academy of Sciences
(2020)
117
Proteome-wide observation of the phenomenon of life on the edge of solubility
G Vecchi, P Sormanni, B Mannini, A Vandelli, GG Tartaglia, CM Dobson, FU Hartl, M Vendruscolo
Proc Natl Acad Sci U S A
(2019)
117
Inherent Biophysical Properties Modulate the Toxicity of Soluble Amyloidogenic Light Chains.
M Maritan, M Romeo, L Oberti, P Sormanni, M Tasaki, R Russo, A Ambrosetti, P Motta, P Rognoni, G Mazzini, A Barbiroli, G Palladini, M Vendruscolo, L Diomede, M Bolognesi, G Merlini, F Lavatelli, S Ricagno
Journal of molecular biology
(2019)
432
Protein Solubility Predictions Using the CamSol Method in the Study of Protein Homeostasis
P Sormanni, M Vendruscolo
Cold Spring Harb Perspect Biol
(2019)
11
Supersaturated Proteins are Enriched at Synapses and Underlie Cell and Tissue Vulnerability in Alzheimer’s Disease
R Freer, P Sormanni, P Ciryam, B Rammner, SO Rizzoli, CM Dobson, M Vendruscolo
Heliyon
(2019)
5
Biochemical and biophysical comparison of human and mouse beta‐2 microglobulin reveals the molecular determinants of low amyloid propensity
A Achour, L Broggini, X Han, R Sun, C Santambrogio, J Buratto, C Visentin, A Barbiroli, CMG De Luca, P Sormanni, F Moda, A De Simone, T Sandalova, R Grandori, C Camilloni, S Ricagno
The FEBS Journal
(2019)
287

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