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

Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-β and α-Synuclein and Suppress the Toxicity of Their Oligomers
R Limbocker, R Staats, S Chia, FS Ruggeri, B Mannini, CK Xu, M Perni, R Cascella, A Bigi, LR Sasser, NR Block, AK Wright, RP Kreiser, ET Custy, G Meisl, S Errico, J Habchi, P Flagmeier, T Kartanas, JE Hollows, LT Nguyen, K LeForte, D Barbut, JR Kumita, C Cecchi, M Zasloff, TPJ Knowles, CM Dobson, F Chiti, M Vendruscolo
Front Neurosci
(2021)
15
Generic nature of the condensed states of proteins
M Fuxreiter, M Vendruscolo
Nature cell biology
(2021)
23
Determination of intermediate state structures in the opening pathway of SARS-CoV-2 spike using cryo-electron microscopy
ZF Brotzakis, T Löhr, M Vendruscolo
Chemical science
(2021)
12
Critical assessment of protein intrinsic disorder prediction.
M Necci, D Piovesan, CAID Predictors, DisProt Curators, SCE Tosatto
Nature methods
(2021)
18
A mistranslation-prone transcriptome underlying polyglutamine expansion diseases
F Buhr, PS Ciryam, M Vendruscolo
Nature Reviews Molecular Cell Biology
(2021)
22
Tau AD fragment aggregates proliferate through autocatalytic secondary nucleation
DR Camargo, E Sileikis, S Chia, E Axell, K Bernfur, R Cataldi, S Cohen, G Meisl, J Habchi, T Knowles, M Vendruscolo, S Linse
(2021)
Comparative Studies in the A30P and A53T α-Synuclein <i>C. elegans</i> Strains to Investigate the Molecular Origins of Parkinson's Disease.
M Perni, A van der Goot, R Limbocker, TJ van Ham, FA Aprile, CK Xu, P Flagmeier, K Thijssen, P Sormanni, G Fusco, SW Chen, PK Challa, JB Kirkegaard, RF Laine, KY Ma, MBD Müller, T Sinnige, JR Kumita, SIA Cohen, R Seinstra, GS Kaminski Schierle, CF Kaminski, D Barbut, A De Simone, TPJ Knowles, M Zasloff, EAA Nollen, M Vendruscolo, CM Dobson
Frontiers in cell and developmental biology
(2021)
9
Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans.
T Sinnige, G Meisl, TCT Michaels, M Vendruscolo, TPJ Knowles, RI Morimoto
Proceedings of the National Academy of Sciences of the United States of America
(2021)
118
Fragment-based computational design of antibodies targeting structured epitopes
MA Rangel, A Bedwell, E Costanzi, R Taylor, R Russo, GJL Bernardes, S Ricagno, J Frydman, M Vendruscolo, P Sormanni
(2021)
Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures
T Ikenoue, FA Aprile, P Sormanni, M Vendruscolo
Front Neurosci
(2021)
15

Co-Director

Research Interest Groups

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01223 763873

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