Alicia holds a degree in Biotechnology from the Polytechnic University of Valencia and a master's degree in Neuroscience from the Complutense University of Madrid. She completed her PhD at the University of Cambridge (St John's College) in 2024 under the supervision of Prof. Michele Vendruscolo, supported by La Caixa Postdoctoral Fellowship. Her doctoral work focused on developing drug screening tools for Alzheimer's disease at the interface of stem cell biology and biophysics. Alongside her PhD, she collaborated for five years with WaveBreak Tx as a research assistant and consultant, contributing to drug discovery programs targeting Alzheimer's and ALS.
Following her doctorate, Alicia was awarded the Alfonso Martín Escudero Fellowship to continue in the Vendruscolo group, before being elected as a Henslow Research Fellow at Hughes Hall. Her research now focuses on engineering next-generation stem cell systems to model sporadic Alzheimer's disease using AI-guided multiplexed funcitonal genomics. She's particularly interested in building "lab-in-the-loop" platforms, where stem cell tools test and inform AI-driven hypotheses in a time- and cost-effective manner. Through this iterative framework, both the experimental models and the algorithms evolve in tandem, bringing cell models ever closer to real patient biology while generating data to power digital twin models of the Alzheimer's disease spectrum.
Ultimately, Alicia's goal is to generate panels of preclinical models of neurodegenerative diseases that accelerate drug discovery and enable personalised medicine. She is also deeply interested in protein phase separation and its role in neuroinflammation in brain disorders.
LIST OF PUBLICATIONS
1. Sneideriene, G.*, González Díaz, A.*, Das Adhikari, S.*, Wei, J., Michaels, T., Sneideris, T., Linse, S., Vendruscolo, M., Garai, K., & Knowles, T. P. J. (2025). The Alzheimer's Aβ peptide forms biomolecular condensates that trigger amyloid aggregation. Proceedings of the National Academy of Sciences,122 (4), e2401307122. https://doi.org/10.1073/pnas.2401307122 (*Co-first author).
2. González Díaz, A., Possenti, A., Urrutia, G. A., Bian, Y., Kedia, S., Boeken, D., Lim, C. M., Licastro, D., Mannini, B., Klenerman, D., & Vendruscolo, M. (2024). A human neuronal model of sporadic Alzheimer's disease induced by FBXO2 downregulation shows Aβ aggregation, tau hyperphosphorylation and functional network impairment. bioRxiv. https://doi.org/10.1101/2024.09.
3. González Díaz, A., Belli, E., Mannini, B., Urrutia, G. A., & Vendruscolo, M. (2024). TNFα-driven Aβ aggregation, synaptic dysfunction and hypermetabolism in human iPSC-derived cortical neurons. bioRxiv. https://doi.org/10.1101/2024.08.
4. González Díaz, A*., Sarracco, E.*, Possenti, A., Kitchen-Smith, I., Chia, S., Menzies, J., Stephenson, G., Cataldi, R., Yahya, K., Bian, Y., & Vendruscolo, M. (2024). In situ generation of Aβ42 oligomers via secondary nucleation triggers neurite degeneration and synaptic dysfunction in human iPSC-derived glutamatergic neurons. bioRxiv. https://doi.org/10.1101/2024.08.
5. González Díaz, A., Cataldi, R., Mannini, B., & Vendruscolo, M. (2024). Preparation and characterization of Zn(II)-stabilized Aβ42 oligomers. ACS Chemical Neuroscience, 15(14), 2586–2599. https://doi.org/10.1021/acschemneuro.4c00084.
6. González Díaz, A., (2024). Building a bridge between biophysics and neurobiology: A synergic approach to develop Alzheimer’s disease translational models and research tools. University of Cambridge. https://doi.org/10.17863/CAM.113748.
7. Lim, C. M.*, & González Díaz, A*. (2024). Identification of phase separating proteins associated with human disease. Nature Reviews Molecular Cell Biology, 25(1), 5. https://doi.org/10.1038/s41580-023-00672-1 (*Co-first author).
8. Lim, C. M.*, González Díaz, A.*, Fuxreiter, M., Pun, F. W., Zhavoronkov, A., & Vendruscolo, M. (2023). Multiomic prediction of therapeutic targets for human diseases associated with protein phase separation. Proceedings of the National Academy of Sciences, 120(40), e2300215120.
https://doi.org/10.1073/pnas.2300215120 (*Co-first author).
9. Ball, S., Hopkins, L., González Díaz, A., Cridland, A., Li, B., B Lee & E., Urrutia, G. A. (2024). Small molecule TDP-43 oligomer/aggregation inhibitor,WTX-245, corrects transcriptional dysfunction across multiple mRNAs in a neuronal cell model for ALS. International Symposium on ALS/MND, Theme 7 Pre-Clinical Therapeutic Strategies. 25(Sup1), 197–217. https://doi.org/10.1080/21678421.2024.2403304.
10. Lim, C. M., Bian, Y., González Díaz, A., Pun, F. W., Zhavoronkov, A., Morimoto, R. & Vendruscolo, M (2025). Organization of the Proteostasis Network of Membraneless Organelles. Advanced Science, vol. 12, no. 33, article e00233. https://doi.org/10.1002/advs.202500233.
11. Brezinova, M., Brotzakis, Z. F., Horne, R. I., Roy Chowdhury, V., Gregory, R. C., Bian, Y., González Díaz, A., Gentile, F. & Vendruscolo, M. (2025) Identification of potent high-affinity secondary nucleation inhibitors of Aβ42 aggregation from an ultra-large chemical library using Deep Docking, Molecular Systems Biology. Molecular Systems Biology, 22, 69–87. https://doi.org/10.1038/s44320-025-00159-5.
12. Chowdhury, V.R., Horne, R.I., González Díaz, A., and Vendruscolo, M., (2024). Secondary pathways cause the proliferation of amyloid aggregates of medin, an aortic medial amyloid peptide associated with cerebral amyloid angiopathy. In FEBS OPEN BIO (Vol. 14, pp. 503-503). 111 RIVER ST, HOBOKEN 07030-5774, NJ USA: WILEY.
13. Baumann, K. N., ŠneiderieneĢ, G., Sanguanini, M., Schneider, M., Rimon, O., González Díaz, A., Greer, H., Thacker, D., Linse, S., & Knowles, T. P. J. (2022). A kinetic map of the influence of biomimetic lipid model membranes on Aβ42 aggregation. ACS Chemical Neuroscience, 14(2), 323–329. https://doi.org/10.1021/acschemneuro.2c00765.
14. Horne, R. I., Wilson-Godber, J., González Díaz, A., Brotzakis, Z. M., Seal, S., Gregory, R. C., Possenti, A., Chia, S., & Vendruscolo, M. (2024). Using generative modeling to endow initially inert compounds with potency, good bioavailability, and low toxicity. J. Chem. Inf. Model. https://doi.org/10.1021/acs.jcim.3c01777.
