Matheus Dornellas Pereira
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Matheus Dornellas Pereira has a total of 6 co-authors. Here are the top co-authors by number of shared publications:
- Airis Farias Santana
Biological Science Department, Instituto Universitario Italiano de Rosario, Corrientes 720, PB y 1er Piso Rosario S2000CTT, Santa Fe, Argentina
1 shared publication - Carolina Passarelli Gonçalves
Postgraduate Program in Chemical Biology, Federal University of São Paulo, Diadema 09913-030, SP, Brazil
1 shared publication - Daniela Gonçalves Rando
Federal University of São Paulo
1 shared publication - Fernanda Sanches Kuhl Antunes
Cosmobeauty, Avenida Aruanã 1160, Barueri 06460-010, SP, Brazil
1 shared publication - Garcia Ferreira de Souza
Biological Science Department, Instituto Universitario Italiano de Rosario, Corrientes 720, PB y 1er Piso Rosario S2000CTT, Santa Fe, Argentina
1 shared publication - Ramon Martins Cogo
Postgraduate Program in Chemical Biology, Universidade Federal de São Paulo, Diadema 09913-030, SP, Brazil
1 shared publication
Latest Publications
- Open Access
- 16 June 2025
- Published by MDPI AG in Pharmaceuticals
- Vol. 18 (6) , 902
Exploring Brazilian Green Propolis Phytochemicals in the Search for Potential Inhibitors of B-Raf600E Enzyme: A Theoretical Approach
Background/Objectives: Melanoma is one of the most aggressive forms of skin cancer and is frequently associated with the B-Raf600E mutation, which constitutively activates the MAPK signaling pathway. Although selective inhibitors such as Vemurafenib offer clinical benefits, their long-term efficacy is often hindered by resistance mechanisms and adverse effects. In this study, twelve phytochemicals from Brazilian green propolis were evaluated for their potential as selective B-Raf600E inhibitors using a computational approach. Methods: Physicochemical, ADME, and electronic properties were assessed, followed by molecular docking using the B-Raf600E crystal structure (PDB ID: 3OG7). Redocking validation and 500 ns molecular dynamics simulations were performed to investigate the stability of the ligand-protein complexes, and free energy calculations were then computed. Results: Among the tested compounds, Artepillin C exhibited the strongest binding affinity (−8.17 kcal/mol) in docking and maintained stable interactions with key catalytic residues throughout the simulation, also presenting free energy of binding ΔG of −20.77 kcal/mol. HOMO-LUMO and electrostatic potential analyses further supported its reactivity and selectivity. Notably, Artepillin C remained bound within the ATP-binding site, mimicking several critical interactions observed with Vemurafenib. Results: Among the tested compounds, Artepillin C exhibited the strongest binding affinity (−8.17 kcal/mol) and maintained stable interactions with key catalytic residues throughout the simulation. HOMO-LUMO and electrostatic potential analyses further supported its reactivity and selectivity. Notably, Artepillin C remained bound within the ATP-binding site, mimicking several critical interactions observed with Vemurafenib. Conclusions: These findings indicate that Artepillin C is a promising natural compound for further development as a selective B-Raf600E inhibitor and suggest its potential utility in melanoma treatment strategies. This study reinforces the value of natural products as scaffolds for targeted drug design and supports continued experimental validation.
- 16 June 2025
- Published by MDPI AG in Pharmaceuticals
- Vol. 18 (6) , 902
Open AccessExploring Brazilian Green Propolis Phytochemicals in the Search for Potential Inhibitors of B-Raf600E Enzyme: A Theoretical Approach
Background/Objectives: Melanoma is one of the most aggressive forms of skin cancer and is frequently associated with the B-Raf600E mutation, which constitutively activates the MAPK signaling pathway. Although selective inhibitors such as Vemurafenib offer clinical benefits, their long-term efficacy is often hindered by resistance mechanisms and adverse effects. In this study, twelve phytochemicals from Brazilian green propolis were evaluated for their potential as selective B-Raf600E inhibitors using a computational approach. Methods: Physicochemical, ADME, and electronic properties were assessed, followed by molecular docking using the B-Raf600E crystal structure (PDB ID: 3OG7). Redocking validation and 500 ns molecular dynamics simulations were performed to investigate the stability of the ligand-protein complexes, and free energy calculations were then computed. Results: Among the tested compounds, Artepillin C exhibited the strongest binding affinity (−8.17 kcal/mol) in docking and maintained stable interactions with key catalytic residues throughout the simulation, also presenting free energy of binding ΔG of −20.77 kcal/mol. HOMO-LUMO and electrostatic potential analyses further supported its reactivity and selectivity. Notably, Artepillin C remained bound within the ATP-binding site, mimicking several critical interactions observed with Vemurafenib. Results: Among the tested compounds, Artepillin C exhibited the strongest binding affinity (−8.17 kcal/mol) and maintained stable interactions with key catalytic residues throughout the simulation. HOMO-LUMO and electrostatic potential analyses further supported its reactivity and selectivity. Notably, Artepillin C remained bound within the ATP-binding site, mimicking several critical interactions observed with Vemurafenib. Conclusions: These findings indicate that Artepillin C is a promising natural compound for further development as a selective B-Raf600E inhibitor and suggest its potential utility in melanoma treatment strategies. This study reinforces the value of natural products as scaffolds for targeted drug design and supports continued experimental validation.