Imperial College London

Dr Francesco A. Aprile

Faculty of Natural SciencesDepartment of Chemistry

Lecturer in Chemistry
 
 
 
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Contact

 

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

 
 
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Location

 

110FMolecular Sciences Research HubWhite City Campus

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Summary

 

Summary

UKRI Future Leaders Fellow 

www.aprilelab.com

RESEARCH INTEREST


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.


OPPORTUNITIES

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.


SELECTED PUBLICATIONS


- 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

Publications

Journals

Ge Y, Masoura A, Yang J, et al., 2022, A Chemical Mutagenesis Approach to Insert Post-Translational Modifications in Aggregation-Prone Proteins, Acs Chemical Neuroscience, ISSN:1948-7193

Thrush RJ, Vadukul D, Aprile F, 2022, A Facile Method to Produce N-Terminally Truncated α-Synuclein, Frontiers in Neuroscience, ISSN:1662-453X

Aprile FA, Temussi PA, Pastore A, 2021, Man does not live by intrinsically unstructured proteins alone: The role of structured regions in aggregation., Bioessays, Vol:43, ISSN:0265-9247, Pages:1-9

Pras A, Houben B, Aprile FA, et al., 2021, The cellular modifier MOAG-4/SERF drives amyloid formation through charge complementation, The Embo Journal, Vol:40, ISSN:0261-4189

Scheidt T, Carozza JA, Kolbe CC, et al., 2021, The binding of the small heat-shock protein alpha B-crystallin to fibrils of alpha-synuclein is driven by entropic forces, Proceedings of the National Academy of Sciences of the United States of America, Vol:118, ISSN:0027-8424, Pages:1-8

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