Tur1A peptide

Tur1A peptide

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

Batch to batch variation of the purity

RRIRFRPPYLPRPGRRPRFPPPFPIPRIPRIP

H-Arg-Arg-Ile-Arg-Phe-Arg-Pro-Pro-Tyr-Leu-Pro-Arg-Pro-Gly-Arg-Arg-Pro-Arg-Phe-Pro-Pro-Pro-Phe-Pro-Ile-Pro-Arg-Ile-Pro-Arg-Ile-Pro-OH

32

95.2%

C₁₈₈H₃₀₀N₆₂O₃₄

3972.78

Synthetic

Powder

Proline-rich antimicrobial peptides (PrAMPs) are antibacterial components of the immune system of some animals. Mardirossian et al. identified two PrAMPs in the artiodactyl Tursiops truncatus (bottlenose dolphin), Tur1A and Tur1B. Tur1A was shown to inhibit bacterial protein synthesis by binding to the ribosome. The proline-rich AMPs Tur1A and Tur1B were identified in the bottlenose dolphin. Tur1A is non-lytic and inhibits bacterial protein synthesis. Tur1A binds within the ribosomal tunnel and prevents translation elongation. Tur1B is a poor inhibitor of translation and thus probably has another target. Peptide truncation indicates that the antimicorbial activity is mainly located at the N-terminal region residues 1-16 (MIC 4 uM). While the intact molecule shows similar activity against sbmA and yjiL KO strains, the truncated peptides 1-16, 8-24, and 16-32 are inactive, indicating the entire sequence do not depend on the Pro-rich peptide transporters for activity. Tur1A inhibits E. coli protein translation by binding to the exit tunnel of ribosome in a reversed order. Interestingly, residues 1-16 plays a major role in ribosome binding.

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

• Cell Chem Biol. 2018 Feb 22. in press. doi: 10.1016/j.chembiol.2018.02.004.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.