J ANDRÉS RIVAS PARDO

I have a deep interest in the emerging topic of Mechano-Biology. From the very first moment that a single cell divides, mechanical forces take place in practically all the fundamental processes of the cell, from chromosome segregation to cell-cell communication. Unlike other cellular inputs, such as electrical and chemical signals, the mechanical cues are propagated between and through cells without the diffusion of molecules. Specific protein structures within the cell are in charge of communicating and transmitting these mechanical signals, proteins that are physically connected form a mechanical network along with the cell. Currently, my research project is focused on understanding the dynamics at the single-molecule level of three elastic proteins: titin, alpha/beta-catenin, and the bacterial adhesive pili protein. Whereas titin—responsible for the elasticity of muscles— and catenin—mechano-transductor of cells— are proteins from eukaryotes, pili are bacterial surface proteins that operate as mechanical anchors mediating the adhesion of pathogenic bacteria to human epitheliums and other substrates.
After completing my training in enzymology and structural biology with Prof. Emilio Cardemil (University of Santiago) and Victoria Guixé (University of Chile), I joined the laboratory of Prof. Julio Fernandez world leader in protein biophysics. During my time at Columbia University, I was trained in the interface between Physics and Biology, collaborating in the developing of new instrumentation and techniques to study the properties of elastic proteins. Taking advantage of my training in enzymology and molecular biology, I participated in the publication of several research articles including: i) the development a new tool for covalent protein immobilization—HaloTag— for atomic force microscopy and magnetic tweezers (Popa et al, JACS, 2016; Popa et al, JACS, 2018); ii) a molecular strategy to interfere with the folding of recently synthesized pili proteins of the human pathogen bacteria S. pyogenes (Rivas-Pardo et al, PNAS, 2018); and iii) a mechanical assay to distinguish protein-ligand binding of Bi-substrate enzymes at the single-molecule level (Rivas-Pardo et al, ACS Nano, 2015). Furthermore, in the recent years, I have actively participated in the study of giant muscle protein titin, studying how posttranslational modifications, such as S-glutathionylation, modulate its elasticity (Alegre-Cebollada, Cell, 2014), and how the Immunoglobulin domains from the I-band generate contractile work (Rivas-Pardo, Cell Reports, 2016; Rivas-Pardo, BiorXiv, 2019).