FARSLA Inhibitors

Rapamycin is an mTOR inhibitor that disrupts the mTORC1 complex, a key regulator of protein synthesis and cell growth. FARSLA activity is linked to protein synthesis; rapamycin's inhibition of mTORC1 can lead to reduced demand for protein synthesis, thereby decreasing FARSLA activity due to lessened substrate availability.

Perhexiline is a carnitine palmitoyltransferase (CPT) inhibitor that impairs fatty acid oxidation. FARSLA is involved in tRNA ligase activity, necessary for protein translation. By limiting the energy supply through fatty acid oxidation, perhexiline indirectly decreases the energy-dependent process of protein synthesis, potentially reducing FARSLA activity.

Metformin activates AMP-activated protein kinase (AMPK), leading to the inhibition of protein synthesis. This occurs due to AMPK's negative effect on mTOR signaling. Inhibition of mTOR reduces protein synthesis demand and subsequently may reduce FARSLA activity by decreasing its involvement in tRNA ligase function.

Oligomycin A is an inhibitor of ATP synthase, the enzyme responsible for ATP production. By inhibiting ATP synthesis, oligomycin A can reduce the energy available for protein synthesis. As FARSLA is directly involved in tRNA ligation during protein synthesis, a decrease in energy availability may indirectly inhibit FARSLA activity.

Triciribine specifically inhibits the Akt pathway, which is involved in cell survival and protein synthesis. Inhibiting Akt can reduce the phosphorylation and activation of substrates required for protein synthesis, leading to a lower demand for FARSLA activity as part of the tRNA ligase process.

2-Deoxy-D-glucose acts as a glycolysis inhibitor by competing with glucose for phosphorylation. By disrupting glycolysis, it reduces the supply of energy necessary for protein synthesis. This energy deficit can lead to a decreased need for FARSLAs function in tRNA ligation for protein synthesis.

Chloroquine is an autophagy inhibitor that prevents the degradation of autophagosomes. Since autophagy recycles amino acids necessary for protein synthesis, inhibition of autophagy can decrease the availability of these amino acids, thus potentially reducing FARSLA activity due to limited substrate accessibility.

Sorafenib targets multiple kinases and has been shown to inhibit the RAF/MEK/ERK pathway. This pathway is involved in cell proliferation and protein synthesis. By inhibiting this pathway, sorafenib can indirectly reduce FARSLA activity by decreasing the overall rate of protein synthesis.

Puromycin is an aminonucleoside antibiotic that causes premature chain termination during protein synthesis. Although it does not specifically inhibit FARSLA, by prematurely terminating protein synthesis, it reduces the demand for FARSLAs role in tRNA ligation.

Rotenone is an inhibitor of the mitochondrial electron transport chain at complex I. By disrupting ATP production, this compound can indirectly reduce FARSLA activity due to a general decrease in the energy available for protein synthesis processes.