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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

Modulators of the plasma membrane protect cells from diverse toxic agents, ranging from protein misfolded oligomers to pore forming agents
R Limbocker, RP Kreiser, LR Sasser, AK Wright, DJ Rinauro, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2022)
121,
350A
Counteraction of amyloid-β aggregation by vitamin A and E metabolites in a crowded environment
P Joshi, S Chia, X Yang, M Perni, J Habchi, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2022)
121,
351A
Comparative study of the affinities of natural aminosterols for lipid membranes and their relation with protection from misfolded protein oligomers
S Errico, L Neri, G Lucchesi, D Odino, G Caminati, A Relini, M Zasloff, M Vendruscolo, F Chiti
– FEBS OPEN BIO
(2022)
12,
128
Sequence-Based Prediction of Ph-Dependent Protein Solubility Using Camsol
M Oeller, R Kang, R Bell, H Ausserwoger, P Sormanni, M Vendruscolo
– SSRN Electronic Journal
(2022)
Universal lab-on-a-chip microfluidic spray deposition for bulk and single-molecule analytical methods on surfaces
AM Miller, SKR Chia, T Hakala, Z Toprakcioglu, M Vendruscolo, FS Ruggeri, TPJ Knowles
– BIOPHYSICAL JOURNAL
(2022)
121,
351A
Kinetic analysis of tau aggregation for drug discovery
DJ Rinauro, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2022)
121,
354A
Small molecule and antibody mediated inhibition of the aggregation of a tau fragment implicit in Alzheimer's disease
TL McKenzie, RP Kreiser, RA Limbocker, DJ Rinauro, M Vendruscolo
– BIOPHYSICAL JOURNAL
(2022)
121,
189A
Common sequence motifs of nascent chains engage the ribosome surface and trigger factor.
A Deckert, AME Cassaignau, X Wang, T Włodarski, SHS Chan, CA Waudby, JP Kirkpatrick, M Vendruscolo, LD Cabrita, J Christodoulou
– Proceedings of the National Academy of Sciences
(2021)
118,
e2103015118
Identification of a Thyroid Hormone Derivative as a Pleiotropic Agent for the Treatment of Alzheimer's Disease.
M Runfola, M Perni, X Yang, M Marchese, A Bacci, S Mero, FM Santorelli, B Polini, G Chiellini, D Giuliani, A Vilella, M Bodria, E Daini, E Vandini, S Rudge, S Gul, MOJ Wakelam, M Vendruscolo, S Rapposelli
– Pharmaceuticals (Basel, Switzerland)
(2021)
14,
1330
Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.
J West, S Satapathy, DR Whiten, M Kelly, NJ Geraghty, E-J Proctor, P Sormanni, M Vendruscolo, JN Buxbaum, M Ranson, MR Wilson
– Science advances
(2021)
7,
eabf7606
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Research Interest Groups

Telephone number

01223 763873

Email address

mv245@cam.ac.uk