Gu-ONNRPVYIPRPRPPHPRL-OH (Gu = N,N,N’,N’-tetramethylGuanidino and O = L-ornithine)
Peptide Purity (HPLC)
Api137, a derivative of the insect-produced antimicrobial peptide apidaecin, arrests terminating ribosomes using a unique mechanism of action. Api137 binds to the Escherichia coli ribosome and traps release factor (RF) RF1 or RF2 subsequent to the release of the nascent polypeptide chain. A high-resolution cryo-EM structure of the ribosome complexed with RF1 and Api137 reveals the molecular interactions that lead to RF trapping. Api137-mediated depletion of the cellular pool of free release factors causes the majority of ribosomes to stall at stop codons before polypeptide release, thereby resulting in a global shutdown of translation termination.
Ideally Api137 Peptide should be stored in a freezer at or below -9C. Api137 Peptide should be refrigerated after reconstitution. For more details, please refer to the manual:Handling and Storage of Synthetic Peptides
- Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017
- bioRxiv preprint doi: https://doi.org/10.1101/2020.05.17.100735. this version posted May 20, 2020.
- Mardirossian M, Barrière Q, Timchenko T, et al. Fragments of the Nonlytic Proline-Rich Antimicrobial Peptide Bac5 Kill Escherichia coli Cells by Inhibiting Protein Synthesis. Antimicrob Agents Chemother. 2018;62(8):e00534-18. Published 2018 Jul 27. doi:10.1128/AAC.00534-18
- Meydan S, Marks J, Klepacki D, et al. Retapamulin-Assisted Ribosome Profiling Reveals the Alternative Bacterial Proteome. Mol Cell. 2019;74(3):481-493.e6
- Adio S, Sharma H, Senyushkina T, et al. Dynamics of ribosomes and release factors during translation termination in E. coli. Elife. 2018
- Florin T, Maracci C, Graf M, et al. An antimicrobial peptide that inhibits translation by trapping release factors on the ribosome. Nat Struct Mol Biol. 2017;24(9):752-757
About TFA salt
Trifluoroacetic acid (TFA) is a strong acid, which is commonly used to cleave synthesized peptides from solid-phase resins and is also used to improve HPLC performance in the peptide purification step. By default, custom peptides are delivered as lyophilized TFA salts, and can contain as much as 10-45% TFA.
TFA in custom peptides can cause inexplicable discrepancies in subsequent assay data. For instance, TFA in nM concentrations has been shown to interfere with cellular assays, inhibiting cellular proliferation in some instances, and increasing cell viability in others . It has also been found to be an unintended allosteric modulator of the glycine receptor, GlyR.
TFA Removal Service is recommended for:
- Peptides that will be used in cellular assays
- Peptides that will be used as APIs or in manufactured products
- For hydrophilic peptides containing numerous basic residues
Related Products / Services
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