skip to content

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

Publications

A maximum caliber approach for continuum path ensembles
PG Bolhuis, ZF Brotzakis, M Vendruscolo
– The European Physical Journal B
(2021)
94,
188
The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces
T Scheidt, JA Carozza, CC Kolbe, FA Aprile, O Tkachenko, MMJ Bellaiche, G Meisl, QAE Peter, TW Herling, S Ness, M Castellana-Cruz, JLP Benesch, M Vendruscolo, CM Dobson, P Arosio, TPJ Knowles
– Proceedings of the National Academy of Sciences of the United States of America
(2021)
118,
e2108790118
New frontiers for machine learning in protein science.
AS Morgunov, K Liis Saar, M Vendruscolo, TPJ Knowles
– Journal of Molecular Biology
(2021)
167232
Assessment of Therapeutic AntibodyTherapeutic antibodiesDevelopabilityDevelopability by Combinations of In Vitro and In SilicoIn silico Methods
A-M Wolf Pérez, N Lorenzen, M Vendruscolo, P Sormanni
– Methods in molecular biology (Clifton, N.J.)
(2021)
2313,
57
The Amyloid-β Pathway in Alzheimer’s Disease
H Hampel, J Hardy, K Blennow, C Chen, G Perry, SH Kim, VL Villemagne, P Aisen, M Vendruscolo, T Iwatsubo, CL Masters, M Cho, L Lannfelt, JL Cummings, A Vergallo
– Mol Psychiatry
(2021)
1
Unraveling the Physicochemical Determinants of Protein Liquid-liquid Phase Separation by Nanoscale Infrared Vibrational Spectroscopy.
FS Ruggeri, AM Miller, M Vendruscolo, TPJ Knowles
– Bio Protoc
(2021)
11,
e4122
Sequence determinants of the aggregation of proteins within condensates generated by liquid-liquid phase separation
M Vendruscolo, M Fuxreiter
– Journal of molecular biology
(2021)
167201
Quantitative Measurement of the Affinity of Toxic and Nontoxic Misfolded Protein Oligomers for Lipid Bilayers and of its Modulation by Lipid Composition and Trodusquemine.
S Errico, H Ramshini, C Capitini, C Canale, M Spaziano, D Barbut, M Calamai, M Zasloff, R Oropesa-Nuñez, M Vendruscolo, F Chiti
– ACS chemical neuroscience
(2021)
12,
3189
Publisher Correction: Two human metabolites rescue a C. elegans model of Alzheimer’s disease via a cytosolic unfolded protein response
P Joshi, M Perni, R Limbocker, B Mannini, S Casford, S Chia, J Habchi, J Labbadia, CM Dobson, M Vendruscolo
– Commun Biol
(2021)
4,
930
Cytosolic aggregation of mitochondrial proteins disrupts cellular homeostasis by stimulating the aggregation of other proteins
U Nowicka, P Chroscicki, K Stroobants, M Sladowska, M Turek, B Uszczynska-Ratajczak, R Kundra, T Goral, M Perni, CM Dobson, M Vendruscolo, A Chacinska
– eLife
(2021)
10,
e65484
  • 1 of 63
  • >

Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk