UKRI Future Leaders Fellow
Our research focusses on the development of biomolecules as research tools to understand disease mechanisms, and for clinical applications.
In particular, we use innovative high-throughput discovery methods to generate antibodies and peptides to study how the complex environment of the nervous system chemically modifies and modulates protein aggregates, called amyloids, which are a hallmark of many forms of dementia.
ABOUT DR APRILE
Dr Aprile obtained his PhD from the University of Milano-Bicocca (Italy) and was previously a Senior Research Fellow of the Alzheimer’s Society in the Department of Chemistry at the University of Cambridge.
We are always looking for curious and talented individuals to work with us. If you are interested in joining our team, please contact us to discuss potential opportunities.
- Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms. De S, Wirthensohn DC, Flagmeier P, Hughes C, Aprile FA, Ruggeri FS, Whiten DR, Emin D, Xia Z, Varela JA, Sormanni P, Kundel F, Knowles TPJ, Dobson CM, Bryant C, Vendruscolo M, and Klenerman D. Nat. Commun. 10, 1541 (2019) doi: 10.1038/s41467-019-09477-3
- Targeting amyloid aggregation: an overview of strategies and mechanisms. Giorgetti S, Greco C, Tortora P, and Aprile FA. Int. J. Mol. Sci. 19, 2677 (2018) doi: 10.3390/ijms19092677
- Selective targeting of primary and secondary nucleation pathways in Aβ42 aggregation using a rational antibody scanning method. Aprile FA, Sormanni P, Perni M, Arosio P, Linse S, Knowles TPJ, Dobson CM, and Vendruscolo M. Sci. Adv. 3, e1700488 (2017) doi: 10.1126/sciadv.1700488
- A rational design strategy for the selective activity enhancement of a molecular chaperone towards a target substrate. Aprile FA, Sormanni P, and Vendruscolo M. Biochemistry 54, 5103-5112 (2015) doi: 10.1021/acs.biochem.5b00459
- Rational design of antibodies targeting specific epitopes within intrinsically disordered proteins. Sormanni P, Aprile FA, and Vendruscolo M. Proc. Natl. Acad. Sci. USA 112, 9902-9907 (2015) doi: 10.1073/pnas.1422401112