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Yusuf Hamied Department of Chemistry

 

Professor of Biophysics

Our research

In the last 15 years our research has been focused on the development of methods of characterising the structure, dynamics and interactions of proteins in previously inaccessible states. These methods are based on the use of experimental data, in particular from nuclear magnetic resonance spectroscopy, as structural restraints in molecular dynamics simulations. Through this approach it is possible to obtain information about a variety of protein conformations, as for example those populated during the folding process, and about protein interactions in complex environments, including those generating aggregate species that are associated with neurodegenerative disorders such as Alzheimer's and Parkinson's diseases.

Application to neurodegenerative diseases

More recently, these studies have led us to investigate the physico-chemical principles of proteins homeostasis and their application to the development of therapeutic strategies against neurodegenerative diseases. Starting from the observation that proteins are expressed in the cell at levels close to their solubility limits, we are developing approaches to prevent or delay misfolding disorders based on the enhancement of our quality control mechanisms against protein aggregation.

Watch Professor Vendruscolo discuss his research

Take a tour of the Una Finlay Laboratory in the Centre for Misfolding Diseases

Publications

Sequence-based virtual screening using transformers.
S Zhang, D Huo, RI Horne, Y Qi, S Pujalte Ojeda, A Yan, M Vendruscolo
– Nature Communications
(2025)
16,
6925
Recruitment of Aβ into α‑Synuclein Condensates Catalyzes Primary Nucleation of α‑Synuclein Aggregation
OM Morris, A Rontgen, Z Toprakcioglu, M Cali, S Dada, M Vendruscolo
– ACS Central Science
(2025)
acscentsci.5c00614
Aβ42 promotes the aggregation of α-synuclein splice isoforms via heterogeneous nucleation.
A Röntgen, Z Toprakcioglu, M Vendruscolo
– FEBS letters
(2025)
1873-3468.70118
Tracking tau and cellular responses in human iPSC-microglia from uptake to seedable secretion in extracellular vesicles
MK Karabova, A del Ser-Badia, A Hedegaard, SJ Washer, Z Baykam, DP O’Brien, I Vendrell, SS Hester, R Fischer, E Johnson, CE Melia, TRS Matthews-Palmer, R Matadeen, A Santambrogio, MA Metrick, M Vendruscolo, S Keeling, KA Xian Cheam, WA McEwan, KS Kosik, TA Day, WS James, SA Cowley
(2025)
Amyloid-β modulates the phase separation and aggregation of α- synuclein
A Röntgen, Z Toprakcioglu, OM Morris, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2025)
122,
e2501987122
Amyloid-β modulates the phase separation and aggregation of α-synuclein
A Röntgen, Z Toprakcioglu, O Morris, M Vendruscolo
– Proceedings of the National Academy of Sciences of the United States of America
(2025)
An aminosterol breaks the autocatalytic cycle of Aβ<sub>42</sub> aggregation and protects cell membranes from its soluble aggregates.
LB Fallot, JR Pinc, JE Buselmeier, JC Palchak, SS Shroff, K Zang, DJ Rinauro, KM Bacon, M Nguyen, MC Schleck, AR Cornell, A Oshidar, DJ Darrell, JM Gabriel, AK Wright, LR Sasser, RP Kreiser, FJ Burpo, A Santambrogio, P Xu, RW Kubiak, J Loverde, VA Jaffett, JR Toole, D Barbut, M Zasloff, F Chiti, AJ Dear, M Vendruscolo, R Limbocker
– Proceedings of the National Academy of Sciences
(2025)
122,
e2417944122
Targeted Protein Modification with an Antibody-Based System
O Rimon, J Konc, I Černauskiene, M Ali, VR Chowdhury, P Sormanni, GJL Bernardes, M Vendruscolo
– ACS Central Science
(2025)
acscentsci.5c00651
Global kinetic model of lipid-induced <i>α</i>-synuclein aggregation and its inhibition by small molecules.
A Stevenson, R Staats, AJ Dear, D Voderholzer, JE Dreier, G Meisl, R Guido, TPJ Knowles, C Galvagnion, AK Buell, M Vendruscolo, TCT Michaels
– Proceedings of the National Academy of Sciences
(2025)
122,
e2422427122
Proteostasis signatures in human diseases
CM Lim, M Vendruscolo
– Plos Computational Biology
(2025)
21,
e1013155
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk