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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

Unraveling the Physicochemical Determinants of Protein Liquid-liquid Phase Separation by Nanoscale Infrared Vibrational Spectroscopy.
FS Ruggeri, AM Miller, M Vendruscolo, TPJ Knowles
– Bio-protocol
(2021)
11,
e4122
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 Chem Neurosci
(2021)
12,
3189
Sequence Determinants of the Aggregation of Proteins Within Condensates Generated by Liquid-liquid Phase Separation: Sequence code of aggregation in protein condensates
M Vendruscolo, M Fuxreiter
– J Mol Biol
(2021)
434,
167201
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
– Communications biology
(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
Modulation of the Interactions Between α-Synuclein and Lipid Membranes by Post-translational Modifications.
R Bell, M Vendruscolo
– Front Neurol
(2021)
12,
661117
Exogenous misfolded protein oligomers can cross the intestinal barrier and cause a disease phenotype in C. elegans
M Perni, B Mannini, CK Xu, JR Kumita, CM Dobson, F Chiti, M Vendruscolo
– Scientific reports
(2021)
11,
14391
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
– Communications biology
(2021)
4,
843
Soluble amyloid beta-containing aggregates are present throughout the brain at early stages of Alzheimer’s disease
DI Sideris, JSH Danial, D Emin, FS Ruggeri, Z Xia, YP Zhang, E Lobanova, H Dakin, S De, A Miller, JC Sang, TPJ Knowles, M Vendruscolo, G Fraser, D Crowther, D Klenerman
– Brain Commun
(2021)
3,
fcab147
Distinct responses of human peripheral blood cells to different misfolded protein oligomers.
M Leal-Lasarte, B Mannini, F Chiti, M Vendruscolo, CM Dobson, C Roodveldt, D Pozo
– Immunology
(2021)
164,
358
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk