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Microsomal triglyceride transfer protein (MTP) inhibitors block the assembly of lipoproteins. MTP is a heterodimer of a large lipid transfer subunit and protein disulfide isomerase in the lumen of the endoplasmic reticulum. It loads triglycerides onto apolipoprotein B (apoB) to form very-low-density lipoproteins in the liver and chylomicrons in the intestine. The protein was found to be absent in abetalipoproteinemia in 1992, a disorder in which apoB-containing lipoproteins are missing from plasma. In 1998 an MTP inhibitor, the compound later named lomitapide, normalized atherogenic lipoprotein levels in Watanabe heritable hyperlipidemic rabbits. Lomitapide, implitapide, dirlotapide and SLX-4090 are inhibitors used to study lipoprotein secretion and dietary fat absorption.
MTP3 ligand-1 is a ligand for the MTP3 target involved in PROTAC-mediated degradation. This compound facilitates the degradation of MYC through the PROTAC MTP3 degrade-1 system, enabling targeted protein degradation studies. MTP3 ligand-1 is essential for elucidating MYC's role in various biological processes and its implications in cancer research and therapeutic development.
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