In SilicoInteractions of the Components from theSchinus terebinthifoliusExtract with Human Tyrosinase

Abstract

The anti‐tyrosinase activity of the leaf extract of Schinus terebinthifolius, also known as Brazilian peppertree, was evaluated using multiple in silico approaches, such as molecular homology, molecular docking, MM‐GBSA, molecular dynamics, MM‐PBSA, QSAR, and skin permeability predictions. With these computational tools, the compounds that downregulate tyrosinase enzyme activity could be evaluated, and more potent molecules could be identified. The results indicated that various compounds, especially luteolin, are accountable for the anti‐tyrosinase activity of S. terebinthifolius. For cosmetic application, further studies with luteolin are especially recommended, for having presented a good performance both in theoretical inhibition (30.92 kJ mol−1) and skin permeability (LogKp=−6.62 cm−1).

Ligands‐induced open‐close conformational change during DapE catalysis: Insights from molecular dynamics simulations

“…Additionally, the absolute values of the binding energies are strongly influenced by the parameters chosen, the charge models, and the simulation length. However, the MMPBSA method offers a reasonable description of the relative binding free energies among different substrates or inhibitors for different Zn 2+ containing proteins 94–96 …”

“…However, the MMPBSA method offers a reasonable description of the relative binding free energies among different substrates or inhibitors for different Zn 2+ containing proteins. [94][95][96]…”