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

Structural defects in amyloid-β fibrils drive secondary nucleation.

J Hu, T Scheidt, D Thacker, E Axell, E Stemme, U Łapińska, S Wennmalm, G Meisl, S Curk, M Andreasen, M Vendruscolo, P Arosio, A Šarić, JD Schmit, TPJ Knowles, E Sparr, S Linse, TCT Michaels, AJ Dear

Nature Communications

(2026)

1933

(doi: 10.1038/s41467-026-69377-1)

Classification of tauopathies from human brain homogenates through salt-modulated tau amplification

A Santambrogio, MA Metrick, P Xu, NCT Gallagher, S Koga, B Ghetti, DW Dickson, B Caughey, M Vendruscolo

Alzheimer's and Dementia

(2026)

e71112

(doi: 10.1002/alz.71112)

Metadiffusion: inference-time meta-energy biasing of biomolecular diffusion models

HYI Lam, S Pujalte Ojeda, M Brezinova, J Hanke, XE Ong, Y Mu, M Vendruscolo

(2026)

(doi: 10.64898/2026.02.10.704873)

Destabilization of Helix III Initiates Early Serum Amyloid A Misfolding by Exposing Its Amyloidogenic Core.

H Nadwa, ZF Brotzakis, A Santucci, D Braconi, M Vendruscolo

The Journal of Physical Chemistry Letters

(2025)

13190

(doi: 10.1021/acs.jpclett.5c03467)

Single-molecule imaging of small aggregates of IAPP in type 2 diabetes serum with rationally-designed antibody-like scaffolds.

J Lin, YP Zhang, S Chia, D Klenerman, P Sormanni, M Vendruscolo

Chem Sci

(2025)

2748

(doi: 10.1039/d5sc01427a)

Multiplex neurodegeneration proteotoxicity platform reveals DNAJB6 promotes non-toxic FUS condensate gelation and inhibits neurotoxicity.

SJ Resnick, S Qamar, P Krishna, V Korobeynikov, H Ausserwoger, A Miller, P Esposito, JA Varela, J Sheng, LH Huang, J Nixon-Abell, S Melore, CW Chung, NF Läubli, S Kapsiani, X Li, J Wang, N Zhang, MM Alam, AS Burguete, TC Swayne, Y Chen, Y-C Liao, NA Shneider, M Vendruscolo, TPJ Knowles, CF Kaminski, FS Ruggeri, GS Kaminski Schierle, P St George-Hyslop, A Chavez

Nature communications

(2025)

10285

(doi: 10.1038/s41467-025-65178-0)

Binding Paths: Describing Small Molecule Interactions with Disordered Proteins via Markov State Models

A Louet, G Hummer, M Vendruscolo

(2025)

(doi: 10.1101/2025.11.19.688850)

Ca²⁺-driven PDIA6 biomolecular condensation ensures proinsulin folding

Y-H Lee, T Saio, M Watabe, M Matsusaki, S Kanemura, Y Lin, T Mannen, T Kuramochi, Y Kamada, K Iuchi, M Tajiri, K Suzuki, Y Li, Y Heo, K Ishii, K Arai, K Ban, M Hashimoto, S Oshita, S Ninagawa, Y Hattori, H Kumeta, A Takeuchi, S Kajimoto, H Abe, E Mori, T Muraoka, T Nakabayashi, S Akashi, T Okiyoneda, M Vendruscolo, K Inaba, M Okumura

Nat Cell Biol

(2025)

1952

(doi: 10.1038/s41556-025-01794-8)