Temporin-1RNb peptide

Temporin-1RNb peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-FLPLKKLRFGLL-NH2

H-Phe-Leu-Pro-Leu-Lys-Lys-Leu-Arg-Phe-Gly-Leu-Leu-NH2

12

95.13%

C₇₃H₁₂₂N₁₈O₁₂

1443.86

Synthetic

Powder

Temporin-1RNb is an antimicrobial peptide isolated from the skin secretions of the black-spotted frog, Rana nigromaculata, Northeastern China, Asia.
Temporin-1RNb belongs to the temporin family of antimicrobial peptides. Temporin-1RNb exhibits strong antimicrobial activity against both Gram-positive and Gram-negative bacteria, as well as the yeast pathogen Candida albicans. Specifically, it is active against E. coli, P. aeruginosa (MIC 12.5 uM), S. aureus, B. cereus, S. lactis (MIC 3.13 uM), C. albicans (MIC 6.25 uM), and cancer cells MCF 7 cells and Hela cells (IC50 ~12 uM). HC50 (50% hemolysis at 136 uM). Temporin-1RNb has a higher antimicrobial potency compared to other temporin peptides, likely due to specific amino acid substitutions.
Temporin-1RNb adopts an extended alpha-helical conformation in a membrane-mimetic environment, indicating its potential to interact with anionic membranes. Temporin-1RNb does not show haemolytic activity against human erythrocytes or toxicity against tested cancer cell lines, suggesting its selective cytotoxic activity against bacteria and cancer cells with negatively charged membranes.
Temporin-1RNb is helical in SDS or TFE.

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

• Li A, Zhang Y, Wang C, Wu G, Wang Z. Purification, molecular cloning, and antimicrobial activity of peptides from the skin secretion of the black-spotted frog, Rana nigromaculata. World J Microbiol Biotechnol. 2013;29(10):1941-9.

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.