Felipe Montecinos, Ph.D. (a.k.a. Dr. Montecinos-Franjola) received his bachelor’s from The University of Chile in Santiago, Chile, in 2006. He joined the graduate research program in biological sciences at the same university in 2007. During this period, Dr. Montecinos studied the function and structure of the conserved protein FtsZ (Filamentous temperature-sensitive protein Z), which plays a pivotal role in bacterial cell division and is an essential target for designing new antibiotics. He used several biophysical techniques to analyze FtsZ structure and its assembly thermodynamics, including chromatography, circular dichroism and fluorescence spectroscopy, time-resolved fluorescence, analytical ultracentrifugation, mathematical modeling, structural modeling, and light and electron microscopy. After publishing his research in international scientific journals, he obtained his doctoral degree in 2012.
In 2013, Dr. Montecinos joined NICHD’s basic and translational biophysics program as a postdoctoral fellow, where he studied the cytoskeletal protein tubulin self-association thermodynamics and interactions with anticancer drugs, using analytical ultracentrifugation and fluorescence spectroscopy. From 2018 to 2019, Dr. Montecinos worked as a postdoctoral scholar at the Physiology and Biophysics Department at the School of Medicine, Case Western Reserve University in Cleveland, Ohio. He studied the role of Dynamin-related protein 1 (DRP1) self-association in mitochondrial fission using fluorescent-protein fusions and live-cell time-resolved laser microscopy combined with autocorrelation analysis. In 2020, Dr. Montecinos joined the Chemistry Department at George Washington University in Washington D.C. as a postdoctoral researcher. He developed new fluorescent protein sensors that emit in the far-red to track cargo translocation across the nuclear membrane, actin cytoskeletal remodeling, mitochondrial fission, and lysosome stability in live cells. In 2021, Dr. Montecinos joined NIDCD’s Structural Cell Biology Section, where he developed the workflow to determine the tridimensional structure of intracellular membrane protein aquaporin-11 using single-particle cryogenic electron microscopy, combined with molecular dynamics simulations of water and hydrogen peroxide transport. He also developed a workflow to study actin cytoskeleton in membranous cellular protrusions using cryotomography and computational reconstructions. In 2023, Dr. Montecinos joined the Protein Expression Laboratory at NIAMS.
Dr. Montecinos’ research in structural biology focuses on studying the tridimensional structure of proteins, their interactions, and how these two aspects enable their functions in the cell. Structural biology aims to understand how newly synthesized proteins fold and to obtain a complete picture of the tridimensional shape of proteins and their complexes. This knowledge is critical for understanding the molecular mechanisms of life and how their dysfunction can cause disease. At the same time, this information can be used to design targeted therapies to treat diseases such as cancer and for treating or preventing viral infections.
In his investigations, Dr. Montecinos uses molecular and cell biology techniques, such as gene expression, mutagenesis, protein purification, and a host of biophysical techniques, including but not limited to chromatography, spectroscopy, light and electron microscopy, mathematical and computational modeling, and simulations. Most recently, Dr. Montecinos has developed expertise in using single-particle analysis with cryogenic electron microscopy to solve the tridimensional structure of isolated protein complexes, and in the context of the living cellular environment, using cryotomography and computational reconstructions.