Seoul National University · Biochemistry, Genetics and Molecular Biology
Professor Jeewoo Lee's research lab specializes in the design and synthesis of bioactive molecules targeting key cellular receptors and signaling pathways involved in cancer and pain. The lab focuses on developing conformationally constrained ligands—particularly for protein kinase C and vanilloid receptors—through innovative scaffold design to enhance binding specificity and metabolic stability. A major research direction involves creating novel HSP90 inhibitors that selectively target the C-terminal domain to overcome limitations of N-terminal inhibitors, such as heat shock response induction and off-target effects. The lab also explores structure-activity relationships to optimize therapeutic potential in cancer stem cells and inflammatory pain pathways.
Figures are computed from collected data and may differ slightly.
Isosteric replacement of the phenolic hydroxyl group in potent vanilloid receptor (VR1) agonists with the alkylsulfonamido group provides a series of compounds which are effective antagonists to the action of the capsaicin on rat VR1 heterologously expressed in Chinese hamster ovary (CHO) cells. In particular, compound 61, N-[2-(3,4-dimethylbenzyl)-3-pivaloyloxypropyl]-N'-[3-fluoro-4-(methylsulfonylamino)benzyl]thiourea was a full antagonist against capsaicin, displayed a K(i) value of 7.8 nM (c
Conformationally constrained analogues of diacylglycerol (DAG) built on a racemic 5(-)[(acyloxy)-methyl]-5-(hydroxymethyl)tetrahydro-2-furanone template were shown previously to have excellent binding affinities for protein kinase C (PK-C). Since the interaction of PK-C with DAG is stereospecific, it was anticipated that PK-C would bind tightly to only one enantiomeric form of the compounds constructed with this new lactone template. Separation of enantiomers by chiral HPLC was discarded due to
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