What we do

Our research group focuses on the study of metal-protein interactions that are relevant in neurodegenerative and degenerative diseases. We use an array of spectroscopic techniques to study metal ion binding to peptides that are prone to aggregation, such as β-amyloid peptide (involved in Alzheimer´s disease), α-synuclein (main protein component in Lewy bodies in Parkinson´s disease), prion protein fragments, amyllin (associated to diabetes type 2) and lens crystallin proteins (associated to cataract disease). Our group is interested in elucidating the coordination and redox chemistry associated to these metal-protein interactions, and in understanding how metal binding impacts local protein folding and aggregation propensity. Our research provides further insights into the biological inorganic chemistry of these degenerative diseases, paving the road towards the design of therapeutic strategies that target the role of metal ions in these pathologies.

Publications

“Tryptophan regulates Drosophila zinc stores”

Garay, E.; Schuth, N.; Barbanente, A.; Tejeda-Guzmán, C.; Vitone, D.; Osorio, B.; Clark, A.H.; Nachtegaal, M.; Haumann, M.; Dau, H.; Vela, A.; Arnesano, F.; Quintanar, L.; Missirlis, F. “Tryptophan regulates Drosophila zinc stores” Proc. Natl. Acad. Sci. USA 2022, 119, 16, e21178071119. https://doi.org/10.1073/pnas.2117807119

“Comparing the copper binding features of alpha and beta synucleins”

Rodríguez-Méndez, E.E.; Ríos, A.; Trujano-Ortiz, L.G.; Villegas, A.; Castañeda-Hernández, G.; Fernández, C.O.; González, F.J.; Quintanar, L. “Comparing the copper binding features of alpha and beta synucleins” J. Inorg. Biochem. 2022, 229, 111715. https://doi.org/10.1016/j.jinorgbio.2022.111715

Meet Our Experts

Lab Members