Biophysical Society Conference | Estes Park 2023

Membrane Budding and Fusion

Poster Abstracts

13-POS Board 5 NATURAL PRODUTS MAY PREVENT THE EFFICIENT BUDDING OF VIRAL PARTICLES Thaina S Rodrigues 1 ; Luana Seixas 1 ; Jessica M Sá 1 ; Isabella Otenio 1 ; Jefferson S Busso 1 ; Luis O Regasini 2 ; Icaro P Caruso 1 ; Marcelo A Fossey 1 ; Fatima P Souza 1 ; 1 1.UNESP, Department of Physics and Multiuser Center of Biomolecular Innovation, Institute of Biosciences, Letters and Exact Sciences, São José do Rio Preto, SP, Brazil 2 2.UNESP, Department of Chemistry,Institute of Biosciences, Letters and Exact Sciences, Sao José do Rio Preto, Brazil The Respiratory Synccytial Virus (RSV) Matrix protein is responsable for a key step in the process for the virus assembles and buds through the plasma membrane, forming elongated membrane filaments through oligomerization and activity of the matrix protein M. This interaction between M and cellular receptors includes proteins involved, cytoskeketon regulation, membrane remodeling, and cellluar trafficking and the positive residual charged on the M protein domains may allow for its interaction with the negatively charged plasma membrane of pneumocytes, which likely serves to interacte with other viral and host proteins. In this context, natural produts have been important and can interact with important binding sites for proteins, preventing their action. The aim of this work was to verify the interaction fo M protein and Coumarin, Resveratrol, Chalcone, and Kaempferol by spectroscopic techniques. The M protein expression was proceeding in Escherichia coli and the protein was purified by affinity and molecular chromatography. The interaction assays were verified by spectroscopy titration. Results showed that Circular Dichroism analysis in the presence of the compound that the binding between them does not involve changes in the secundary structure of the protein.The fluorescence spectroscopy showed that Sterm-Volmer constant is the order of 104 M-1 and the dissociation contant is the order 104 M-1 for Coumarin, Resveratrol, Chalcone, and Kaempherol withe similar values in the same order of interation. The thermodinamic analysis showed a hydrophobic binding for all ligands and the stoichiometry (n) of 1 ligand per protein. In conclusion, these molecules can act on the interaction of M protein monomers preventing the process of oligomerization and, consequently to prevent the budding process of the viral particle and thus prevent the success of an ongoing infection. Financial support: FAPESP, FINEP, CNPQ and Capes

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