CV Lattes
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Universidade de São Paulo (USP). Faculdade de Ciências Farmacêuticas de Ribeirão Preto (FCFRP) (Institutional affiliation from the last research proposal) Birthplace: Brazil
Assistant Professor at the Faculty of Pharmaceutical Sciences of Ribeirão Preto of the University of São Paulo (FCFRP-USP). Has experience in Structural Biology/Molecular Biophysics, in the study of protein/peptide structure and dynamics through techniques such as solution NMR, X-ray crystallography, small-angle X-ray scattering circular dichroism and molecular modeling. Bachelor in Physical and Biomolecular Sciences at the Institute of Physics of São Carlos (IFSC) of the University of São Paulo (USP) (2009-2012) with scientific initiation supervised by Prof. Dr. Claudia Munte. He was awarded the Bernhard Gross Award for the best academic performance (2012). Doctorate degree at the Institute of Physics of São Carlos (2013-2018), with a doctoral scholarship from the São Paulo Research Foundation (FAPESP) and under supervision of Prof. Dr. Richard Garratt. In his doctorate, he did a sandwich period at Universitaet Regensburg, Germany, in the laboratory of Prof. Dr. Dr. Hans Kalbitzer using high-pressure NMR to characterize rare conformations of the beta-amyloid peptide (2011-2012). Postdoctoral fellow at the IFSC studying coiled coils of septins, a family of cytoskeletal proteins, under Prof. Garratt supervision (2019-2023). Postdoctoral fellow at the University of Bristol, UK, under the supervision of Prof. Dr. Matthew Crump (2022-2023). (Source: Lattes Curriculum)
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Septins constitute a conserved guanine-binding protein family which are involved in several cellular processes and are capable of self-assembling into heterofilaments and high-order complexes. The human septins are encoded by 13 different genes and are divided into four groups based on their similarity. The C-terminal domain of septins contains characteristic repeats of alpha-helix coiled…
The main histological feature in Alzheimer's disease is the presence of amyloid plaques in patient's brain. The most abundant element of these plaques is the beta-amyloid peptide (Abeta). The peptide is produced through a proteolytic cleavage of the amyloid precursor protein (APP), resulting predominantly in the Abeta(1-40) and Abeta(1-42) forms, the latter being the more toxic species. I…
Cystatins are inhibitors of cysteine proteases. The majority are only weak inhibitors of human cathepsin B, which has been associated with cancer, Alzheimer's disease and arthritis. Starting from the sequences of oryzacystatin-1 and canecystatin-1, a hybrid clone was recently obtained, which presented higher inhibitory activity towards cathepsin B. This clone presented two unanticipated …
Septins are membrane-associated GTP-binding proteins which are important in a wide range of physiologically essential processes such as cytokinesis, microtubule dynamics, formation of diffusion barriers and mechanotransduction. The importance of the coiled-coil domains in the formation and maintenance of septin complexes is still not fully understood. It has been almost 15 years since the…
The main histological feature in Alzheimer's disease is the presence of amyloid plaques in patient's brain. The most abundant element of these plaques is the beta-amyloid peptide (Abeta). The peptide is produced through a proteolytic cleavage of the amyloid precursor protein (APP), resulting predominantly in the Abeta(1-40) and Abeta(1-42) forms, the latter being the more toxic species. I…
| 1 / 1 | Completed research grants |
| 3 / 3 | Completed scholarships in Brazil |
| 2 / 2 | Completed scholarships abroad |
| 6 / 6 | All research grants and scholarships |
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