RAIMON SABATE LAGUNAS

RAIMON SABATE LAGUNAS

Senior lecturer

ORCID: 0000-0003-3894-2362
Scopus Author ID: 6602786140
Researcher ID: I-7849-2014
Knowledge area: Química Física

Research group:

  • PhotoBioCat
  • Fisiopatologia, Hemostàsia i Trombosi

Contact Information
Department of Pharmacy and Pharmaceutical Technology and Physical Chemistry
Secció de Fisicoquímica. Departament de Farmàcia, Tecnologia Farmacèutica i Fisicoquímica. Facultat de Farmàcia i Ciències de l'Alimentació. Joan XXIII 27-31 08020-Barcelona
934035986
rsabate(a)ub.edu

Academic training

Llicenciat en Farmàcia

Research interests

In the cell, the biological function is determined for the native protein fold. In this way, problems in the protein fold with the consequent apparition of misfolded species can disturb the essential cellular processes. Importantly, the protein misfolding entailing the polypeptide aggregation into amyloid structures have been associated with dozens of human diseases as Alzheimer, Parkinson or prion diseases. Interestingly, recent studies have shown that the amyloid aggregation process is not limited to disease-related proteins but appears to be a generic property of the proteins in both eukaryotic and prokaryotic cells. The possibility that the amyloid formation is a universal and omnipresent process shared for all life organisms entails important consequences in biology. Prions are naturally occurring proteins that, after a conformational conversion, self-assemble into β-sheet enriched amyloid-like structures and become self-perpetuating in vivo, acting as pathological infectious agents or protein-based genetic elements. So, prion protein (PrP) is related to transmissible spongiform encephalopathy (TSE); fatal neurodegenerative diseases that effects from sheets ("scrapie") and crows (bovine spongiform encephalopathy bovina) or ("mad crow") to humans (Creutzfeldt-Jakob)

Relevant publications

Eraña, H.; Charco, J.M.; Di-Bari, M.A.; Díaz-Domínguez, C.M.; López-Moreno, R.; Vidal, E.; González-Miranda, E.; Pérez-Castro, M.A.; García-Martínez, S.; Bravo, S.; Fernández-Borges, N.; Geijo, M.; D'Agostino, C.; Garrido, J.; Bian, J.; König, A.; Uluca-Yazgi, B.; Sabate, R.; Khaychuk, V.; Vanni, I.; Telling, G.C.; Heise, H.; Nonno, R.; Requena, J.R.; Castilla, J. Development of a New largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies. In PLoS Pathogens. Volume 15. Number 10. 2019 . Institutional Repository
Caballero, A. B.; Iranzo, O.; Hautier, A.; Sabate, R.; Gamez, P. Peptidic Scaffolds To Reduce the Interaction of Cu(II) Ions with beta-Amyloid Protein. In Inorganic Chemistry. Volume 59. Number 1. 2020 . https://doi.org/10.1021/acs.inorgchem.9b03099
Espargaró, A.; Llabrés, S.; Saupe, S.J.; Curutchet, C.; Luque, F.J.; Sabaté, R. On the Binding of Congo Red to Amyloid Fibrils. In Angewandte Chemie-International Edition. Volume 59. Number 21. 2020 . Institutional Repository
Matesanz, Ana I.; Caballero, Ana B.; Lorenzo, Carmen; Espargaro, Alba; Sabate, Raimon; Quiroga, Adoracion G.; Gamez, Patrick. Thiosemicarbazone Derivatives as Inhibitors of Amyloid-beta Aggregation: Effect of Metal Coordination. In Inorganic Chemistry. Volume 59. Number 10. 2020 . https://doi.org/10.1021/acs.inorgchem.0c00467
Kowalczyk, J.; Grapsi, E.; Espargaró, A.; Caballero, A.B.; Juárez-Jiménez, J.; Busquets, MA.; Gamez, P.; Sabate, R.; Estelrich, J. Dual effect of Prussian Blue nanoparticles on Aβ40 aggregation: β-sheet fibril reduction and copper dyshomeostasis regulation. In Biomacromolecules. Volume 22. Number 2. 2021 . https://doi.org/10.1021/acs.biomac.0c01290
Caterina Pont; Tiziana Ginex; Christian Griñan-Ferre; Matthias Scheiner; Alexia Mattellone; Noemí Martínez; Elsa M. Arce; Yolanda Soriano-Fernandez; Marina Naldi; Angela De Simonef; Marta Barenys; Jesús Gómez-Catalán; Belen Perez; Raimon Sabate; Vincenza Andrisano; María Isabel Loza; Jose Brea; Manuela Bartolini; Maria Laura Bolognesi; Michael Decker; Merce Pallas; F. Javier Luque; Diego Muñoz-Torrero. From virtual screening hits targeting a cryptic pocket in BACE-1 to a nontoxic brain permeable multitarget anti-Alzheimer lead with disease-modifying and cognition-enhancing effects. In European Journal of Medicinal Chemistry. Volume 225. Number 113779. 2021 . Institutional Repository
Peŕez-Areales,F. J.; Garrido, M.; Aso, E.; Bartolini, M.; DeSimone,A.; Espargaro, A.,́ Ginex, T.; Sabate,R.; Peŕez, B.; Andrisano, V.; Puigoriol-Illamola, D.; Pallas̀, M.; Luque, F. J.; Loza, M. I.; Brea, J.; Ferrer, I.; Ciruela, F.; Messeguer, A.; Muñoz-Torrero, D. Centrally active multitarget anti-Alzheimer agents derived from the antioxidant lead CR‐6. In Journal of Medicinal Chemistry. Volume 63. 2020 . https://doi.org/10.1021/acs.jmedchem.0c00528
Wichur, T.; Pasieka, A.; Godyń, J.; Panek, D.; Góral, I.; Latacz, G.; Honkisz-Orzechowska, E.; Bucki, A.; Siwek, A.; Głuch-Lutwin, M.; Knez, D.; Brazzolotto, X.; Gobec, S.; Kołaczkowski, M.; Sabate, R.; Malawska, B.; Więckowska, A. Discovery of 1-(phenylsulfonyl)-1H-indole-based multifunctional ligands targeting cholinesterases and 5-HT 6 receptor with anti-aggregation properties against amyloid-beta and tau. In European Journal of Medicinal Chemistry. 2021
Alvarez-Berbel, I.; Espargaró, A.; Viayna, A.; Caballero, A. B.; Busquets, M. A.; Gamez, P.; Luque, F. J.; Sabate, R. Three to tango: Inhibitory Effect of quercetin and apigenin on acetylcholinesterase, amyloid-β aggregation and acetylcholinesterase-amyloid interaction. In Pharmaceutics. Volume 14. Number 11. 2022 . Institutional Repository
Tonelli M.; Catto M.; Sabaté R.; Francesconi V.; Laurini E.; Pricl S.; Pisani L.; Miniero D.V.; Liuzzi G.M.; Gatta E.; Relini A.; Gavín R.; Del Rio J.A.; Sparatore F.; Carotti A. Thioxanthenone-based derivatives as multitarget therapeutic leads for Alzheimer's disease. In European Journal of Medicinal Chemistry. Volume 250. 2023 . https://doi.org/10.1016/j.ejmech.2023.115169

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