| Grant number: | 16/24452-6 |
| Support type: | Scholarships abroad - Research Internship - Post-doctor |
| Effective date (Start): | March 01, 2017 |
| Effective date (End): | February 28, 2018 |
| Field of knowledge: | Biological Sciences - Biophysics - Molecular Biophysics |
| Principal Investigator: | Antonio José da Costa Filho |
| Grantee: | Luís Guilherme Mansor Basso |
| Supervisor abroad: | Stanley J. Opella |
| Home Institution: | Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto (FFCLRP). Universidade de São Paulo (USP). Ribeirão Preto , SP, Brazil |
| Local de pesquisa : | University of California, San Diego (UC San Diego), United States |
| Associated to the scholarship: | 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides, BP.PD |
Abstract The current research proposal is an extension of the FAPESP PD fellowship hold by Dr. Luís Basso and aims at describing the activities to be performed by the candidate during his stay at the University of California, San Diego (UCSD), under the supervision of Prof. Dr. Stanley Opella, an internationally recognized leader in the field of membrane protein structural determination by solid-state nuclear magnetic resonance (ssNMR) spectroscopy. Due to the inherent difficulties in deriving structural information at atomic resolution of membrane peptides embedded in native cell-like lipid bilayers, we will take advantage of Prof. Opella's expertise to work with the fusion peptides (FP) from SARS-CoV Spike glycoprotein in lipid model membranes. We have previously shown that SARS FPs dehydrate and bend lipid bilayers, giving new insights on the peptide-mediated mechanism of membrane fusion (paper recently accepted in Scientific Reports). However, the active fusion peptide conformation and its topology in membranes along with the molecular details of the peptide-induced membrane curvature and dehydration remain elusive. Therefore, we aim at determining atomic resolution data of the structure, orientation, and the degree of peptide insertion into lipid bilayers under nearly physiological conditions by using modern high-resolution ssNMR methods. That information is crucial to understand the mechanism of peptide action, since there is a high correlation between secondary structure and membrane insertion depth with FP's fusogenic activity. | |