Our research group focuses in the study of metal-protein interactions that are relevant in degenerative diseases
What We Do
Solid phase peptide synthesis
Solid phase peptide synthesis
Spectroscopic studies of metal -protein interactions
Peptide and Protein purification
Recombinant protein expression
Spectroscopic analysis of biological coordination complexes
Peptide and Protein purification
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.
Latest Publications
A new Cu2+-binding 1,3-benzodioxole-containing N-Acylhydrazone protects Saccharomyces cerevisiae cells from oxidative stress
Marinho-Barbosa, B.; Pires, C.D.; Galvácsi, A.; Gaudard, A. J.; Flores, L. S.; Sánchez-López, C.; Correa, C. C.; Cukierman, D.S.; Hureau, C.; Kállay, C.; Pereira, M.D.; Quintanar, L.; Rey, N. A. “A new Cu2+-binding 1,3-benzodioxole-containing N-Acylhydrazone protects Saccharomyces cerevisiae cells from oxidative stress.” ChemistrySelect 2025, 10, e202405195. https://doi.org/10.1002/slct.202405195
Read MoreA copper-binding peptide with therapeutic potential against Alzheimer´s disease: From the blood-brain barrier to metal competition
López-Guerrero, V.E.; Posadas, Y.; Sánchez-López, C.; Smart, A.; Miranda, J.; Singewald, K.; Bandala, Y.; Juaristi, E.; Den Auwer, C.; Perez-Cruz, C.; González-Mariscal, L.; Millhauser, G.; Segovia, J.; Quintanar, L. “A copper-binding peptide with therapeutic potential against Alzheimer´s disease: From the blood-brain barrier to metal competition” ACS Chemical Neuroscience 2025, 16, 241-261. https://doi.org/10.1021/acschemneuro.4c00796
Read MoreIn situ detection of ferric reductase activity in the intestinal lumen of an insect
Hernández-Gallardo, A.; Arcos-López, T.; Bahena-Lopez, J.; Tejeda-Guzmán, C.; Webb, S.M Kroll, T.; Solari, P.-L.; Sánchez-López, C.; den Auwer, C.; Quintanar, L.; Missirlis, F. “In situ detection of ferric reductase activity in the intestinal lumen of an insect.” J. Biol. Inorg. Chem. 2024, 29, 773-784. https://doi.org/10.1007/s00775-024-02080-y
Read MoreAn N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: A molecular dynamics study
Gómez-Castro, C.Z.; Quintanar, L.; Vela, A.; “An N-terminal acidic β-sheet domain is responsible for the metal-accumulation properties of amyloid-β protofibrils: A molecular dynamics study” J. Biol. Inorg. Chem. 2024, 29, 407-425. https://doi.org/10.1007/s00775-024-02061-1
Read MoreCopper binding and protein aggregation: a journey from the brain to the human lens
Posadas, Y.; Sánchez-López, C.; Quintanar, L. “Copper binding and protein aggregation: a journey from the brain to the human lens” RSC Chem.Biol. 2023, 4, 974-985. https://doi.org/10.1039/D3CB00145H
Read MoreAn ATCUN-like copper site in 𝛽B2-crystallin plays a protective role in cataract-associated aggregation
Tovar, M.; Schuth, N.; Rodríguez-Meza, O.Kroll, T.; Saab-Rincon, G.; Costas, M.; Lampi, K.; Quintanar, L. “An ATCUN-like copper site in 𝛽B2-crystallin plays a protective role in cataract-associated aggregation” Inorg. Chem. 2023, 62, 27, 10592-10604. https://doi.org/10.1021/acs.inorgchem.3c00794
Read MoreMeet Our Experts
Lab Members
