TINP1 Inhibitors
Chemical inhibitors of TINP1 can effectively shut down its role in ribosome biogenesis by targeting various stages of protein synthesis. Cycloheximide, a well-known inhibitor, disrupts the translocation step on the eukaryotic ribosome, which is crucial for the elongation of nascent protein chains. This action directly reduces the cellular demand for new ribosomes, thereby inhibiting the functionality of TINP1. Similarly, harringtonine and homoharringtonine obstruct early stages of protein synthesis: harringtonine by preventing the initial elongation after the first peptide bond is formed, and homoharringtonine by binding to the A-site of the ribosome, blocking the elongation process. Anisomycin's inhibition of peptidyl transferase activity also contributes to the reduction of ribosomal activity, diminishing the need for TINP1's involvement in ribosome assembly.
Further down the protein synthesis pathway, ricin and α-sarcin exert their effects by damaging the ribosome's RNA, ricin by depurinating adenine from rRNA and α-sarcin by cleaving a specific bond in the rRNA, both results in the inactivation of the ribosomes. This inactivation directly negates the function of TINP1, as it can no longer contribute to the assembly of functional ribosomes. Edeine and fusidic acid target the initiation and elongation steps, respectively, with edeine binding to the small ribosomal subunit, preventing the formation of the initiation complex, and fusidic acid by locking elongation factor G onto the ribosome, preventing its turnover. Puromycin, sparsomycin, and tetracycline achieve their effects by mimicking aminoacyl-tRNA causing premature chain termination, binding to the peptidyl transferase center to inhibit peptide bond formation, and binding to the 30S subunit to prevent aminoacyl-tRNA attachment, respectively. Chloramphenicol binds to the 50S subunit, also inhibiting peptidyl transferase.
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 eukaryotic protein synthesis by interfering with the translocation step in the ribosome, thereby preventing the elongation of the nascent protein chain. This would inhibit TINP1 as it is involved in ribosome biogenesis, and the inhibition of protein synthesis would decrease the demand for new ribosomes, thereby functionally inhibiting TINP1. | ||||||
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 after the formation of the first peptide bond on the 60S ribosome. This would functionally inhibit TINP1 by halting ribosome biogenesis at an early stage, as TINP1 is involved in the assembly and maturation of ribosomes. | ||||||
Homoharringtonine | 26833-87-4 | sc-202652 sc-202652A sc-202652B | 1 mg 5 mg 10 mg | $52.00 $125.00 $182.00 | 11 | |
Homoharringtonine inhibits protein synthesis by binding to the A-site of the ribosome, which prevents the proper elongation of the peptide chain. As TINP1 is crucial for ribosome biogenesis, the inhibition of ribosomal function would directly decrease the functional need for TINP1 activity. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $99.00 $259.00 | 36 | |
Anisomycin inhibits peptidyl transferase activity on ribosomes, leading to the inhibition of protein synthesis. By blocking peptide bond formation, anisomycin functionally inhibits TINP1 by reducing the requirement for ribosomal biogenesis, where TINP1 is essential. | ||||||
α-Sarcin | 86243-64-3 | sc-204427 | 1 mg | $462.00 | 6 | |
α-Sarcin cleaves a specific phosphodiester bond in the larger rRNA of the ribosome, which inactivates the ribosome and inhibits protein synthesis. As TINP1 is involved in ribosomal assembly, the loss of ribosomal function would functionally inhibit TINP1. | ||||||
Fusidic acid | 6990-06-3 | sc-215065 | 1 g | $292.00 | ||
Fusidic acid inhibits protein synthesis by preventing the turnover of elongation factor G (EF-G) from the ribosome. This would functionally inhibit TINP1 as it would lead to a reduced requirement for new ribosomes, thereby inhibiting TINP1's role in ribosome biogenesis. | ||||||
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 translation by acting as an analog to aminoacyl-tRNA. This would functionally inhibit TINP1 by reducing the need for ribosome production and assembly, processes in which TINP1 is involved. | ||||||
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 ribosome and inhibits the binding of aminoacyl-tRNA to the A site of the ribosome. This would functionally inhibit TINP1 by impeding the elongation phase of protein synthesis, thereby reducing the demand for ribosome biogenesis where TINP1 is necessary. | ||||||
Chloramphenicol | 56-75-7 | sc-3594 | 25 g | $90.00 | 10 | |
Chloramphenicol binds to the 50S ribosomal subunit and inhibits peptidyl transferase activity, thereby inhibiting protein synthesis. This would functionally inhibit TINP1 by decreasing the overall production of ribosomes, diminishing the functional requirement for TINP1 in ribosome assembly. | ||||||