"CANCELLED: Orthogonal fingerprinting for accurate and fast mechanical characterization of proteins by AFM"
Who: Jorge Alegre Cebollada, CNIC, Madrid
Place: Donostia International Physics Center
Date: Monday, 14 May 2018, 12:00
host: David de Sancho at DIPC
The seminar has been moved to another venue. See details below:
Data / Fecha: 2018ko maiatzak 14 / 14 de mayo de 2018
Ordua / Hora: 13:00.
Lekua / Lugar: Biodonostia OIIko Prestakuntza Aretoan, 3.Solairua. / IIS Biodonostia, Sala de Formación, Planta 3.
Hizlaria / Ponente: Dr Jorge Alegre-Cebollada. Group Leader ? Molecular Mechanics of the Cardiovascular System. National Institute of Cardiovascular Research (CNIC), Madrid.
Argibide gehiago / Más información:
Laburpena / Resumen:
My lab focuses on understanding emergent mechanical properties of proteins that sustain the function of the heart. Advancements in single-molecule techniques have provided fundamental insights into how proteins behave when placed under a pulling force. However, we still do not know much about how protein nanomechanics manifests at the cell and tissue levels. One of our current lines of research is to examine the role of redox signalling in the modulation of biomechanics in vivo. We have found that titin, a giant protein that is the main responsible for the passive elasticity of striated muscle, forms disulfide bonds in vivo, which are strong modulators of titin?s mechanical properties. Now, we are examining whether titin oxidation is affected by heart diseases, such as myocardial infarction, that lead to alterations both of the redox state of the myocardium and its stiffness. We have also observed that mutations causing cardiomyopathies induce nanomechanical phenotypes, which we hypothesize can lead to altered mechanical function of the target protein. This project requires exquisite accuracy in the determination of protein nanomechanical properties, which has led us to the development of a new single-molecule methodology called orthogonal fingerprinting. Finally, we have implemented a simplified model system based on protein biomaterials to be able to test hypotheses on how nanomechanical properties of proteins emerge from the nano to the macroscale.