A series of novel indole-based PPAR agonists is described leading to discovery of 10k, a highly potent PPAR pan-agonist. The structural biology and molecular docking studies revealed that the distances between the acidic group and the linker, when a ligand was complexed with PPARγ protein, were important for the potent activity. The hydrophobic tail part of 10k makes intensive hydrophobic interaction with the PPARγ protein resulting in potent activity.
|Number of pages||5|
|Journal||Journal of Medicinal Chemistry|
|Publication status||Published - Feb 9 2006|
ASJC Scopus subject areas
- Organic Chemistry