Imperial College London

Dr Francesco A. Aprile

Faculty of Natural SciencesDepartment of Chemistry

Future Leadership Fellow



+44 (0)20 7594 5545f.aprile Website




110FMolecular Sciences Research HubWhite City Campus





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.


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:

- 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



Ikenoue T, Aprile FA, Sormanni P, et al., 2020, A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer's disease., Sci Rep, Vol:10

Aprile FA, Sormanni P, Podpolny M, et al., 2020, Rational design of a conformation-specific antibody for the quantification of A beta oligomers, Proceedings of the National Academy of Sciences of the United States of America, Vol:117, ISSN:0027-8424, Pages:13509-13518

Limbocker R, Mannini B, Cataldi R, et al., 2020, Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-beta Oligomers, International Journal of Molecular Sciences, Vol:21

Faravelli G, Raimondi S, Marchese L, et al., 2019, C. elegans expressing D76N β2-microglobulin: a model for in vivo screening of drug candidates targeting amyloidosis., Sci Rep, Vol:9

Lindstedt PR, Aprile FA, Matos MJ, et al., 2019, Enhancement of the Anti-Aggregation Activity of a Molecular Chaperone Using a Rationally Designed Post-Translational Modification, Acs Central Science, Vol:5, ISSN:2374-7943, Pages:1417-1424

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