EF-1 ε1 Inhibitors
Chemical inhibitors of EF-1 ε1 can function through various mechanisms, primarily by disrupting the process of protein synthesis at different stages. Cycloheximide is a well-known inhibitor that targets the translocation step in protein synthesis within eukaryotic cells, directly affecting the elongation phase where EF-1 ε1 is active. By preventing the elongation of polypeptide chains, cycloheximide effectively inhibits the function of EF-1 ε1. Similarly, anisomycin disrupts protein synthesis by inhibiting peptidyl transferase activity in ribosomes, which is essential for peptide chain elongation, thus indirectly inhibiting the activity of EF-1 ε1. Ricin, a potent ribosome-inactivating protein, depurinates a specific adenine residue in ribosomal RNA, critically important for the binding of elongation factors, and this action precludes EF-1 ε1 from performing its role in translation elongation.
Furthermore, emetine and puromycin act as inhibitors by binding to the ribosomal subunits and mimicking aminoacyl-tRNA, respectively. Emetine's binding to the 40S subunit obstructs the ribosomal movement along mRNA, while puromycin induces premature chain termination, both resulting in the functional inhibition of EF-1 ε1. Tetracycline and chloramphenicol, although primarily targeting bacterial ribosomes, would, by a similar mechanism, affect eukaryotic cells by preventing aminoacyl-tRNA from binding to the ribosome's A site and by inhibiting peptidyl transferase activity, respectively. This would result in an indirect inhibition of EF-1 ε1's function in protein elongation. Fusidic acid, which inhibits the turnover of elongation factor G in bacteria, would also, by a similar mechanism, disrupt the overall process of protein synthesis, affecting the function of EF-1 ε1. Additionally, harringtonin prevents the initial elongation step of translation, thereby directly inhibiting the function of EF-1 ε1. α-Sarcin achieves inhibition by cleaving a specific bond in the ribosomal RNA, inhibiting the binding of elongation factors to the ribosome, which includes EF-1 ε1. Sparsomycin and lycorine both interfere with the ribosome's ability to form peptide bonds and proceed with the elongation phase. Sparsomycin binds directly to the peptidyl transferase cavity, while lycorine disrupts both initiation and elongation phases of protein synthesis.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Cycloheximide | 66-81-9 | sc-3508B sc-3508 sc-3508A | 100 mg 1 g 5 g | $41.00 $84.00 $275.00 | 127 | |
Cycloheximide inhibits protein synthesis in eukaryotic organisms by interfering with the translocation step in protein synthesis, thus preventing the elongation of the polypeptide. This would functionally inhibit EF-1 ε1 by preventing it from contributing to the elongation of growing peptide chains during mRNA translation. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin acts as a protein synthesis inhibitor by blocking peptidyl transferase activity in eukaryotic ribosomes. By disrupting this function, the activity of EF-1 ε1, which is involved in the elongation phase of translation, would be indirectly inhibited as the overall process of translation is halted. | ||||||
Emetine | 483-18-1 | sc-470668 sc-470668A sc-470668B sc-470668C | 1 mg 10 mg 50 mg 100 mg | $440.00 $900.00 $1400.00 $2502.00 | ||
Emetine inhibits protein synthesis by binding to the ribosomal 40S subunit, blocking the movement of the ribosome along the mRNA. This inhibition of translation would indirectly inhibit the function of EF-1 ε1, which is required for the elongation phase of protein synthesis. | ||||||
Puromycin dihydrochloride | 58-58-2 | sc-108071 sc-108071B sc-108071C sc-108071A | 25 mg 250 mg 1 g 50 mg | $42.00 $214.00 $832.00 $66.00 | 394 | |
Puromycin causes premature chain termination during protein synthesis by acting as an analog of aminoacyl-tRNA, thus inhibiting the elongation process in which EF-1 ε1 is involved. Once bound to the ribosome, puromycin prevents EF-1 ε1 from delivering the correct aminoacyl-tRNA to the ribosome. | ||||||
Tetracycline | 60-54-8 | sc-205858 sc-205858A sc-205858B sc-205858C sc-205858D | 10 g 25 g 100 g 500 g 1 kg | $63.00 $94.00 $270.00 $417.00 $634.00 | 6 | |
Tetracycline binds to the 30S subunit of the bacterial ribosome, inhibiting the binding of aminoacyl-tRNA to the A site of the ribosome. While it primarily affects bacteria, if it were to have an effect on eukaryotic cells, it would indirectly inhibit EF-1 ε1's function in translation. | ||||||
Chloramphenicol | 56-75-7 | sc-3594 | 25 g | $90.00 | 10 | |
Chloramphenicol binds to the 50S ribosomal subunit and inhibits peptidyl transferase activity, which would indirectly inhibit the function of EF-1 ε1 by stopping the ribosome from elongating protein chains during translation. | ||||||
Fusidic acid | 6990-06-3 | sc-215065 | 1 g | $292.00 | ||
Fusidic acid prevents the turnover of elongation factor G (EF-G) from the ribosome, indirectly inhibiting the protein synthesis process. Although EF-G is different from EF-1 ε1, the inhibition of one elongation factor can disrupt the overall translation process, which would affect the function of EF-1 ε1. | ||||||
Harringtonin | 26833-85-2 | sc-204771 sc-204771A sc-204771B sc-204771C sc-204771D | 5 mg 10 mg 25 mg 50 mg 100 mg | $250.00 $367.00 $548.00 $730.00 $980.00 | 30 | |
Harringtonine inhibits protein synthesis by preventing the initial elongation step of translation. This would functionally inhibit EF-1 ε1 by blocking its role in the elongation phase of protein synthesis. | ||||||
α-Sarcin | 86243-64-3 | sc-204427 | 1 mg | $462.00 | 6 | |
α-Sarcin cleaves a specific bond at the ribosomal RNA's sarcin-ricin loop, ultimately inhibiting the binding of elongation factors like EF-1 ε1 to the ribosome, thereby inhibiting protein synthesis. | ||||||