Scientific researcher of the CSIC at the Cajal Institute of Neurobiology (Madrid) where he leads the Laboratory of Protein Nanomechanics.
He has a B.S. in biology (with a major in biochemistry) from the University of Valencia and a doctorate from the Autonomous University of Madrid. His postdoctoral stay in the laboratory of Prof. Julio Fernández focused mainly on the establishment of a new field that they named “Protein Nanomechanics”, first as a postdoctoral researcher at the Mayo Clinic (Rochester, MN, USA) and later as an associate scientist at Columbia University (New York, NY, USA).
His general interest has been essentially the understanding of the inner workings of proteins, one of the great pending subjects of biology. From the technological point of view, he was the first researcher to apply protein engineering in force spectroscopy studies (using atomic force microscopy), a technological combination that was key for the progress of the field of protein nanomechanics. Dr. Carrión-Vázquez established the main model systems used in the field of protein nanomechanics: the I27 titin module and ubiquitin. He also developed the methodology of “polyproteins” as markers of individual molecules and demonstrated the capacity of force spectroscopy as a quantitative tool for the direct study of the mechanical properties of proteins. More recently, he has developed a new strategy (“mechanical protection”) for the unequivocal identification of single-molecule events, which solves most of the technical problems in protein nanomechanics, particularly for the case of proteins with conformational polymorphism.
Among its scientific achievements, it is worth highlighting the discovery of the proteins with the highest mechano-stability described to date: the cohesin I modules of scaffoldins (in folded proteins) and the hyper-mechanostable conformations of neurotoxic proteins (in intrinsically disordered proteins). Furthermore, he has discovered the universality of the mechanical motif that they have called “mechanical clamp” and characterized the nanomechanical properties of the most relevant modules (Ig, FIII, cadherins, cohesins) in modular proteins (titin, fibronectin, cadherins, scaffoldins) and of several key proteins in biology (ubiquitin, neurotoxic proteins, functional prionoids). Finally, he has discovered the conformational polymorphism of neurotoxic proteins as a common feature (exacerbated in pathology) to all amyloids at the beginning of the amyloidogenesis cascade and the polyvalence of the QBP1 peptide as an inhibitor of amyloidogenesis in several neurodegenerative diseases and in the consolidation of memory.His scientific work has been reflected in important publications in international journals and books as well as national and international patents. He has been an evaluator for numerous national and international institutions and coordinator of national and European projects.At present, his laboratory focuses fundamentally on the study of the molecular bases of three fundamental processes: memory, neurodegeneration and biocatalysis. In particular, they study amyloids, both pathological (neurotoxic proteins, implicated in neurodegenerative diseases) and functional (CPEB, a prionoid involved in memory consolidation through the tagging of active synapses), and scaffolding proteins (which coordinate enzymatic cascades). His lines of research have a double scope, fundamental and applied.