Professor Michele Vendruscolo

University position
Professor
Professor Michele Vendruscolo is pleased to consider applications from prospective PhD students.
Departments
Home page
http://www-vendruscolo.ch.cam.ac.uk/index.html
Research Theme
Interests
My research is aimed at taking full advantage of an approach that exploits effectively the synergy between experiment and theory in order to advance towards a full characterisation of the process of protein aggregation.
We have developed a method (http://www-vendruscolo.ch.cam.ac.uk/zyggregator.php) based on the simple physico-chemical characteristics of the amino acids, that enables predictions to be made about several aspects of the process of peptide and protein aggregation.
We are using this approach to investigate a model of Alzheimer’s disease based on the expression of the Abeta peptide in Drosophila melanogaster as an “in vivo test tube” in which to probe the molecular determinants of protein aggregation and its biological consequences.
We also have recently revealed a very close connection between two important but distinct aspects of the behaviour of proteins in the cell - their aggregation propensities and the expression levels of the corresponding genes

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Research Focus
Keywordsamyloid protein aggregation computational methods |
Clinical conditionsAlzheimer's disease |
Equipment
Computational modelling
Collaborators
CambridgeDavid Lomas | InternationalFabrizio Chiti Web: http://www.fabriziochiti.it/ |
Key publications
Tartaglia GG, Pechmann S, Dobson CM and Vendruscolo M (2007), “Life on the Edge: A link between gene expression levels and aggregation rates of human proteins” Trends Biochem Sci 32:204-206 Details
Pawar AP, DuBay KF, Zurdo J, Chiti F, Vendruscolo M and Dobson CM (2005), “Prediction of aggregation-prone and aggregation-susceptibl regions in proteins associated with neurodegenerative diseases” J Mol Biol 350:379-392 Details
DuBay KF, Pawar AP, Chiti F, Zurdo J, Dobson CM and Vendruscolo M (2004), “Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains” J Mol Biol 341:1317-1326 Details


