Api137 Peptide

Api137 Peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

Gu-ONNRPVYIPRPRPPHPRL-OH (Gu = N,N,N’,N’-tetramethylGuanidino and O = L-ornithine)

18

93.95%

C₁₀₄H₁₇₁N₃₇O₂₂

2291.4

Synthetic

Powder

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.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. 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

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.