The class
Lead benzylamino-methanone compound achieves 30 percent CETP inhibition at 10 micromolar (Molecules 2010)
Original title: Design, synthesis, and biological evaluation of benzylamino-methanone based cholesteryl ester transfer protein inhibitors
Guided by previously reported pharmacophore and QSAR models for CETP inhibition, researchers synthesized and bioassayed a new series of benzylamino-methanone compounds targeting cholesteryl ester transfer protein, the glycoprotein that shuttles lipoprotein particles and neutral lipids between HDL and LDL and is considered a valid target for treating dyslipidemia. The most potent compound in the series achieved 30% CETP inhibition at a 10 micromolar concentration, establishing benzylamino-methanones as a modest but structurally distinct addition to the CETP inhibitor medicinal chemistry landscape.
Original abstract
Cholesteryl ester transfer protein (CETP) is a glycoprotein involved in transporting lipoprotein particles and neutral lipids between high-density lipoprotein (HDL) and low density lipoproteins (LDL) and therefore its a proper target for treating dyslipidemia and related disorders. Guided by our previously-reported pharmacophore and QSAR models for CETP inhibition, we synthesized and bioassayed a series of benzylamino-methanones. The most potent illustrated 30% CETP inhibition at 10 microM.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.