Luis Felipe Santos Mendes

Luis Felipe Santos Mendes is an Associated Professor at the Group of Biophysics and Structural Biology "Sergio Mascarenhas" - São Carlos Institute of Physics, University of São Paulo. I received a Bachelor's in Biomolecular Physics in 2011 from the IFSC/USP and a PhD (2018) in Physics Applied to Medicine and Biology in the FFCLRP/USP. As a PhD student in the FFCLRP/USP, I was part of a structural biology project involving a multitasking protein called GRASP, which plays essential roles in the Golgi maintenance and Unconventional Secretory Pathways. During the PhD, I spent one year as a guest student in the Biomembrane Structure Unit of the University of Oxford-UK (supervision of Prof. Dr Anthony Watts), two months in the Lab. für Physikalische Chemie - ETH Zurich (supervision of Prof. Dr Gunnar Jeschke) and one month in the Chemistry Department of NCSU (guidance of Prof. Dr Alex I. Smirnov). The PhD thesis was selected, by the Brazilian Physical Society, as the best one in the Biological Physics field defended during the biennial 2017/2018. I was also a postdoctoral fellow in the BioNMR group at the Department of Chemistry and Applied Biosciences of the Swiss Federal Institute of Technology (ETH) Zurich and in the Physics Department of the FFCLRP/USP (2018-2022). Elucidating the intricated unstructured biology of Intrinsically disordered proteins (IDPs) and protein hybrids that contain both ordered and intrinsically disordered protein regions (IDPRs) is still challenging, which we address using a range of biophysical/biochemical methods. We are particularly interested in the fundamental nature of the native, droplet, and amyloid states of these proteins. These different states are relevant in biology because proteins are near the supersaturation limits at their typical cellular concentrations in physiological conditions. Therefore, most proteins can populate all these states under native cellular conditions and interconvert between them. That is why protein condensates can be found not only in pathology (like in amyotrophic lateral sclerosis, Alzheimer's and Parkinson's diseases) but also having positive/functional roles in life, including the origin of life itself. I have experience in classical molecular biology methodologies (cloning, subcloning, mutant construction, expression/purification of heterologous soluble/membrane proteins and Ancestor Sequence Reconstruction) and several spectroscopic and calorimetric techniques, including Circular Dichroism (conventional and synchrotron-radiation), fluorescence (steady-state and lifetime techniques), Magnetic Resonances (electronic and nuclear) and Differential Scanning Fluorimetry and Calorimetry (DSF and DSC).

Luis Felipe Santos Mendes is an Associated Professor at the Group of Biophysics and Structural Biology "Sergio Mascarenhas" - São Carlos Institute of Physics, University of São Paulo. I received a Bachelor's in Biomolecular Physics in 2011 from the IFSC/USP and a PhD (2018) in Physics Applied to Medicine and Biology in the FFCLRP/USP. As a PhD student in the FFCLRP/USP, I was part of a structural biology project involving a multitasking protein called GRASP, which plays essential roles in the Golgi maintenance and Unconventional Secretory Pathways. During the PhD, I spent one year as a guest student in the Biomembrane Structure Unit of the University of Oxford-UK (supervision of Prof. Dr Anthony Watts), two months in the Lab. für Physikalische Chemie - ETH Zurich (supervision of Prof. Dr Gunnar Jeschke) and one month in the Chemistry Department of NCSU (guidance of Prof. Dr Alex I. Smirnov). The PhD thesis was selected, by the Brazilian Physical Society, as the best one in the Biological Physics field defended during the biennial 2017/2018. I was also a postdoctoral fellow in the BioNMR group at the Department of Chemistry and Applied Biosciences of the Swiss Federal Institute of Technology (ETH) Zurich and in the Physics Department of the FFCLRP/USP (2018-2022). Elucidating the intricated unstructured biology of Intrinsically disordered proteins (IDPs) and protein hybrids that contain both ordered and intrinsically disordered protein regions (IDPRs) is still challenging, which we address using a range of biophysical/biochemical methods. We are particularly interested in the fundamental nature of the native, droplet, and amyloid states of these proteins. These different states are relevant in biology because proteins are near the supersaturation limits at their typical cellular concentrations in physiological conditions. Therefore, most proteins can populate all these states under native cellular conditions and interconvert between them. That is why protein condensates can be found not only in pathology (like in amyotrophic lateral sclerosis, Alzheimer's and Parkinson's diseases) but also having positive/functional roles in life, including the origin of life itself. I have experience in classical molecular biology methodologies (cloning, subcloning, mutant construction, expression/purification of heterologous soluble/membrane proteins and Ancestor Sequence Reconstruction) and several spectroscopic and calorimetric techniques, including Circular Dichroism (conventional and synchrotron-radiation), fluorescence (steady-state and lifetime techniques), Magnetic Resonances (electronic and nuclear) and Differential Scanning Fluorimetry and Calorimetry (DSF and DSC).. More about our lab: https://sites.google.com/usp.br/unstructuralbiology