UKRI Future Leaders Fellow
Our research focuses 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.
- Rationally Designed Antibodies as Research Tools to Study the Structure–Toxicity Relationship of Amyloid-β Oligomers. Limbocker R, Mannini B, Cataldi R, Chhangur S, Wright AK, Kreiser RP, Albright JA, Chia S, Habchi J, Sormanni P, Kumita JR, Ruggeri FS, Dobson CM, Chiti F, Aprile FA and Vendruscolo M. Int. J. Mol. Sci. 21, 4542 (2020) doi: https://doi.org/10.3390/ijms21124542
- Rational design of a conformation-specific antibody for the quantification of Aβ oligomers. Aprile FA, Sormanni P, Podpolny M, Chhangur S, Needham LM, Ruggeri FS, Perni M, Limbocker R, Heller GT, Sneideris T, Scheidt T, Mannini B, Habchi J, Lee SF, Salinas PC, Knowles TPJ, Dobson CM and Vendruscolo M. Proc. Natl. Acad. Sci. USA (2020) doi: 10.1073/pnas.1919464117
- 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
et al., 2021, The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces., Proc Natl Acad Sci U S A, Vol:118
et al., 2021, Modulation of amyloid-beta aggregation by metal complexes with a dual binding mode and their delivery across the blood-brain barrier using focused ultrasound, Chemical Science, Vol:12, ISSN:2041-6520, Pages:9485-9493
et al., 2021, The diagnostic potential of amyloidogenic proteins, International Journal of Molecular Sciences, Vol:22, ISSN:1422-0067
et al., 2021, Comparative studies in the A30P and A53T alpha-Synuclein C. elegans strains to investigate the molecular origins of Parkinson's Disease, Frontiers in Cell and Developmental Biology, Vol:9, ISSN:2296-634X, Pages:1-10
et al., 2021, Rationally Designed Bicyclic Peptides Prevent the Conversion of A beta 42 Assemblies Into Fibrillar Structures, Frontiers in Neuroscience, Vol:15