ACAT-3 Inhibitors

N-[3-(4-hydroxyphenyl)-1-oxo-2-propenyl]-L-phenylalanine, methyl ester exhibits intriguing characteristics as an ACAT-3 inhibitor. Its structural conformation allows for specific hydrogen bonding interactions with key residues in the enzyme's active site, enhancing binding affinity. The compound's unique steric properties may alter the enzyme's dynamics, potentially leading to altered substrate accessibility and influencing lipid metabolism pathways. Its kinetic profile suggests a competitive inhibition mechanism, impacting lipid droplet formation and cellular lipid trafficking.

Avasimibe inhibits ACAT-3 by directly binding to the enzyme, thereby obstructing the esterification of cholesterol.

Pyripyropene A functions as an ACAT-3 inhibitor through its distinctive molecular architecture, which facilitates precise interactions with the enzyme's catalytic site. This compound's unique hydrophobic regions promote enhanced affinity, potentially stabilizing enzyme-substrate complexes. Its influence on reaction kinetics suggests a non-competitive inhibition model, which may disrupt lipid homeostasis by modulating the enzymatic processing of cholesterol esters, thereby affecting cellular lipid distribution.

3,4-Dihydroxy Hydrocinnamic acid (L-Aspartic acid dibenzyl ester) amide acts as an ACAT-3 inhibitor by engaging in specific hydrogen bonding and hydrophobic interactions with the enzyme's active site. Its structural features allow for selective binding, influencing the conformational dynamics of the enzyme. This compound may alter lipid metabolism pathways by modulating the rate of cholesterol esterification, thereby impacting cellular lipid profiles and distribution mechanisms.

Terpendole C functions as an ACAT-3 inhibitor through its unique ability to form stable π-π stacking interactions and van der Waals forces with the enzyme's active site. Its distinct molecular architecture facilitates selective recognition, potentially altering enzyme kinetics and substrate affinity. This compound may influence lipid homeostasis by disrupting cholesterol esterification processes, thereby affecting lipid droplet formation and cellular lipid distribution.

A 922500 acts as an ACAT-3 inhibitor by engaging in specific hydrogen bonding and hydrophobic interactions within the enzyme's active site. Its unique structural features enable it to modulate enzyme conformation, potentially enhancing substrate accessibility. This compound may also impact lipid metabolism by altering the dynamics of cholesterol transport and storage, thereby influencing cellular lipid profiles and membrane integrity.

CI-976 inhibits ACAT-3 by binding to the enzyme and blocking its activity, preventing the formation of cholesteryl esters.

F-1394 inhibits ACAT-3 by allosterically altering the enzyme's conformation, which leads to a decrease in its esterification function.

FR-900520 inhibits ACAT-3 by interacting with the enzyme's active site, preventing the conversion of cholesterol to cholesteryl esters.

YIC-C8-434 inhibits ACAT-3 by competitively inhibiting the enzyme, thereby blocking the esterification of cholesterol.