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Yusuf Hamied Department of Chemistry

 

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.

Selected publications

 

 

Dr Sormanni discusses his research

Tour of the Sormanni lab

Publications

Multi-dimensional protein solubility optimization with an ultra-high-throughput microfluidic platform
N Erkamp, M Oeller, T Sneideris, H Ausserwӧger, A Levin, T Welsh, R Qi, D Qian, H Zhu, P Sormanni, M Vendruscolo, TPJ Knowles
(2022)
An antibody scanning method for the detection of α-synuclein oligomers in the serum of Parkinson's disease patients
K Kulenkampff, D Emin, R Staats, YP Zhang, L Sakhnini, A Kouli, O Rimon, E Lobanova, CH Williams-Gray, FA Aprile, P Sormanni, D Klenerman, M Vendruscolo
– Chemical Science
(2022)
13,
13815
Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes.
H Mikolajek, M Weckener, ZF Brotzakis, J Huo, EV Dalietou, A Le Bas, P Sormanni, PJ Harrison, PN Ward, S Truong, L Moynie, DK Clare, M Dumoux, J Dormon, C Norman, N Hussain, V Vogirala, RJ Owens, M Vendruscolo, JH Naismith
– Proc Natl Acad Sci U S A
(2022)
119,
e2205412119
π-Clamp-Mediated Homo- and Heterodimerization of Single-Domain Antibodies via Site-Specific Homobifunctional Conjugation.
RJ Taylor, M Aguilar Rangel, MB Geeson, P Sormanni, M Vendruscolo, GJL Bernardes
– Journal of the American Chemical Society
(2022)
144,
13026
Editorial: Intrinsically Disordered Proteins and Regions: The Challenge to the Structure-Function Relationship
A Toto, P Sormanni, C Paissoni, VN Uversky
– Frontiers in molecular biosciences
(2022)
9,
962643
Automated optimisation of solubility and conformational stability of antibodies and proteins
A Rosace, A Bennett, M Oeller, M Mortensen, L Sakhnini, N Lorenzen, C Poulsen, P Sormanni
(2022)
Conformational Entropy as a Potential Liability of Computationally Designed Antibodies.
T Löhr, P Sormanni, M Vendruscolo
– Biomolecules
(2022)
12,
718
An aggregation inhibitor specific to oligomeric intermediates of Aβ42 derived from phage display libraries of stable, small proteins
S Linse, P Sormanni, DJ O'Connell
– Proc Natl Acad Sci U S A
(2022)
119,
e2121966119
Sequence-based pH-dependent prediction of protein solubility using CamSol
M Oeller, R Kang, P Sormanni, M Vendruscolo
(2022)
Sequence-based prediction and measurement of pH-dependent protein solubility
M Oeller, P Sormanni, M Vendruscolo
– Biophysical Journal
(2022)
121,
350a
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Research Group

Research Interest Group

Email address

ps589@cam.ac.uk

College

Clare Hall