Lf-CATH2 peptide

Lf-CATH2 peptide

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

H-GKCNVLCQLKQKLRSIGSGSHIGSVVLPRG-OH

H-Gly-Lys-Cys-Asn-Val-Leu-Cys-Gln-Leu-Lys-Gln-Lys-Leu-Arg-Ser-Ile-Gly-Ser-Gly-Ser-His-Ile-Gly-Ser-Val-Val-Leu-Pro-Arg-Gly-OH

30

95.44%

C₁₃₄H₂₃₆N₄₄O₃₈S₂

3135.69

Synthetic

Powder

Lf-CATH2 is a mature antimicrobial peptide (AMP) found in the amphibian Limnonectes fragilis. It is one of the two cathelicidins identified in this species, the other being Lf-CATH1. Lf-CATH2 is composed of 30 amino acids and has a higher percentage of alpha-helical structure compared to Lf-CATH1. Both Lf-CATH1 and Lf-CATH2 exhibit potent antimicrobial activities against a broad spectrum of microorganisms, including drug-resistant strains, while showing minimal hemolysis and cytotoxicity, making thempromising cadidates for antimicrobial applications. The antimicrobial activity of Lf-CATH1 appears to be stronger than that of Lf-CATH2, suggesting that the optimal percentage of alpha-helical structure may vary for different peptides.
Details: The sequence of Lf-CATH2 is 56.3% similar to Cathelicidin-PY. Lf-CATH2 is active against Gram-positive S. aureus (ATCC2592, IS1303, IS 1349) (MIC 2.27-9.08 uM), S. epidermidis (MIC 4.5 uM), P. acnes ATCC11827 (MIC 18.2 uM), Gram-negative P. aeruginosa (IS 1411, IS 1412, IS 1413) (MIC 4.5-9.1 uM), E. coli (ATCC25922, IS 1334, IS 1335, IS 1342) (MIC 2.3-9.1 uM), and fungi C. albicans ATCC2002, C. glabrata IS0902) (MIC 1.1-4.5 uM). Lf-CATH2 was found in fragile large-headed frog, fragile wart frog, Limnonectes fragilis, Hainan, China, Asia.

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

• Yu H, Cai S, Gao J, et al. Identification and polymorphism discovery of the cathelicidins, Lf-CATHs in ranid amphibian (Limnonectes fragilis). FEBS J. 2013;280(23):6022-32.
• Lu Y, Gao J, Qiao X, Wang Y, Yu H. [Construction of novel thioredoxin fusion protein expression system and the production of recombinant Lf-CATH2]. Sheng Wu Gong Cheng Xue Bao. 2015 Mar;31(3):403-10.

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.