Jorge Ripoll obtained his BSc in Biology from the University of A Coruña (UC) (2006) and his PhD degree in Molecular Biology and Biomedicine from the University of Cantabria (UC) (2013). All his postdoctoral stage period was done in Portugal under the supervision of Dr. Pedro J.B. Pereira first in IBMC-Instituto de Biologia Molecular e Celular (2014-2016) and later in i3S-Instituto de Investigação e Inovacão em Saúde (2016-2022). He was awarded with a postdoctoral fellowship (2015-2018) of the FCT-Portuguese Funding Agency for Science, Research and Technology. He worked as a Junior Research contract level (2019-2022) and after that he benefited from an Associate Research contract in 2022 through an individual competitive call funded also by FCT. In the 2021 year’s call of the Spanish Agency of Science he obtained a Ramón y Cajal contract that allow him to join the IBBTEC institute as an independent researcher in 2023. 

During his postdoctoral work he specialized in the fields of structural biology, enzymology and biophysical characterization of proteins and he mainly participated in two different projects. In the first one, he investigated the biochemical and structural characterization of mycobacterial proteins involved on an unexplored biosynthetic pathway amenable to therapeutic intervention. As a results of this research, the functional and structural mechanisms that the vast majority of mycobacteria use to produce essential polysaccharides for cell envelope assembly were revealed. In the second project, he studied different thrombin inhibitors based on natural anticoagulants from blood-feeding organisms. He found a new class of molecules amenable to tyrosine sulfation that bind both the active site and the exosite II region of the proteinase, the latter through this post-translational modification. Tyrosine sulfation proved to be crucial to modulate their anticoagulant activities, independently of their thrombin binding mechanism, and its role can be mimicked by sulfonate analogues. Moreover, hybrid variants engineered based on these sulfated scaffolds provided a novel class of functional trivalent inhibitors with improved potency.

His research career is motivated by the functional understanding of clinically relevant biological systems at the molecular level, with the ultimate goal of developing new therapeutics. His current research line aims to develop new anticoagulants able to act against unexplored targets and/or through a different mechanism of intervention.