Ribosomal Protein L23 Inhibitors

Ribosomal Protein L23 (RPL23) inhibitors encompass a diverse array of compounds that intricately modulate the intricate machinery of protein synthesis. These inhibitors primarily target distinct facets of the translation process, disrupting the seamless flow of polypeptide chain elongation orchestrated by the ribosome. Puromycin, an aminonucleoside antibiotic, exemplifies direct inhibition by prematurely terminating peptide elongation, hindering RPL23 engagement in protein synthesis. Additionally, anisomycin and cycloheximide, pyrrole-derived and glutarimide antibiotics, respectively, disrupt the translation process by binding to ribosomal subunits, indirectly influencing RPL23 function. Moreover, aminoglycoside antibiotics such as pactamycin, kasugamycin, and streptovaricin exert their inhibitory effects by interfering with the 30S ribosomal subunit, indirectly modulating RPL23's involvement in translation. Nucleoside antibiotics like blasticidin S and aureothricin disrupt the peptidyl transferase activity of the 60S subunit, indirectly affecting RPL23's role in protein synthesis. Additionally, macrolide antibiotic kitasamycin impedes bacterial protein synthesis by binding to the 50S subunit, indirectly influencing RPL23 during translation.

Furthermore, hygromycin B and nourseothricin, aminoglycoside antibiotics, disrupt protein synthesis by inhibiting translocation on the 70S ribosome. This interference indirectly impacts RPL23, altering its engagement in the translation process. Dactinomycin, an antineoplastic antibiotic, illustrates indirect inhibition by binding to DNA, disrupting RNA synthesis, and influencing cellular processes that indirectly affect RPL23 during protein synthesis. In conclusion, the diverse chemical landscape of RPL23 inhibitors showcases their intricate modes of action, ranging from direct interference with ribosomal subunits to disrupting essential cellular processes. This nuanced understanding opens avenues for exploring targeted interventions in protein synthesis through meticulous modulation of RPL23 function.