  Peroxisome proliferator-activated receptors gamma (PPAR{\gamma}) are
ligand-activated controllers of various metabolic actions and insulin
sensitivity. PPAR{\gamma} is thus considered as an important target to treat
type 2 diabetes. Available PPAR{\gamma} drugs (full agonists) have robust
insulin-sensitizing properties but are accompanied by severe side effects
leading to complicated health problems. Here, we have used molecular docking
and a molecular dynamics simulation study to find a novel PPAR{\gamma} ligand
from a natural product. Our study suggests that the inhibition of ceramicine B
in the PPAR{\gamma} ligand-binding domain (LBD) could act as a partial agonist
and block cdk5-mediated phosphorylation. This result may provide an opportunity
for the development of new anti-diabetic drugs by targeting PPAR{\gamma} while
avoiding the side effects associated with full agonists.
