The class
Amino-acid-modified fungal pigment derivatives yield micromolar, non-competitive CETP inhibitors (Nat Prod Res 2014)
Original title: Novel derivatives of monascus pigment having a high CETP inhibitory activity
Researchers produced orange monascus pigment via fermentation of a Monascus species and synthesised derivative compounds by incorporating 19 different L-amino acids into the pigment, then tested them for CETP inhibitory activity. The L-threonine and L-tyrosine derivatives showed the highest inhibitory activity against CETP, with the effect increasing in a dose-dependent manner to give IC50 values of 1.0 and 2.3 micromolar respectively. Both derivatives inhibited CETP non-competitively, with inhibition constant (Ki) values of 2.7 and 4.3 micromolar respectively. The findings identify amino-acid-modified monascus pigment derivatives as a novel natural-product source of CETP inhibitors for anti-atherosclerosis drug development.
Original abstract
The cholesteryl ester transfer protein (CETP), inhibition of which assists in maintaining a high level of high-density lipoprotein cholesterol in the blood, is a target for anti-atherosclerosis treatments. Orange monascus pigment was produced by a Monascus species in a 5 L jar fermenter and various derivative compounds were synthesised by incorporating 19 different L-amino acids into the orange pigment. Among them, the L-Thr and L-Tyr derivatives exhibited high inhibitory activities against the CETP reaction. The inhibitory activities of the L-Thr and L-Tyr derivatives increased in a dose-dependent manner, resulting in IC50 values of 1.0 and 2.3 μM, respectively. When CETP reactions in the presence of the derivatives were performed, the inhibition modes of the L-Thr and L-Tyr derivatives were non-competitive with inhibition constant (Ki) values of 2.7 and 4.3 μM, respectively.
Summary written by cetpinhibition.org from the published abstract; figures as published. Page updated 19 August 2026. Methods.