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Yusuf Hamied Department of Chemistry

Portrait of mv245

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


A mistranslation-prone transcriptome underlying polyglutamine expansion diseases.
F Buhr, PS Ciryam, M Vendruscolo
– Nat Rev Mol Cell Biol
Interactions of alpha-synuclein oligomers with lipid membranes
G Musteikytė, AK Jayaram, CK Xu, M Vendruscolo, G Krainer, TPJ Knowles
– Biochimica et Biophysica Acta (BBA) - Biomembranes
Comparative Studies in the A30P and A53T α-Synuclein C. elegans 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
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
– Proc Natl Acad Sci U S A
Rationally Designed Bicyclic Peptides Prevent the Conversion of Aβ42 Assemblies Into Fibrillar Structures
T Ikenoue, FA Aprile, P Sormanni, M Vendruscolo
– Frontiers in neuroscience
A structural ensemble of a tau-microtubule complex reveals regulatory tau phosphorylation and acetylation mechanisms
F Brotzakis, P Lindstedt, R Taylor, G Bernardes, M Vendruscolo
Quantifying misfolded protein oligomers as drug targets and biomarkers in Alzheimer and Parkinson diseases
K Kulenkampff, AM Wolf Perez, P Sormanni, J Habchi, M Vendruscolo
– Nature Reviews Chemistry
The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.
WK Man, B Tahirbegi, MD Vrettas, S Preet, L Ying, M Vendruscolo, A De Simone, G Fusco
– Nat Commun
A beta Oligomers Dysregulate Calcium Homeostasis by Mechanosensitive Activation of AMPA and NMDA Receptors
G Fani, B Mannini, G Vecchi, R Cascella, C Cecchi, CM Dobson, M Vendruscolo, F Chiti
– ACS Chem Neurosci
Infrared nanospectroscopy reveals the molecular interaction fingerprint of an aggregation inhibitor with single Aβ42 oligomers
FS Ruggeri, J Habchi, S Chia, RI Horne, M Vendruscolo, TPJ Knowles
– Nat Commun
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01223 763873

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