Brevinin-1LT2 peptide

Brevinin-1LT2 peptide

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

Batch to batch variation of the purity

H-FFGSVLKVAAKVLPAALCQIFKKC-OH

H-Phe-Phe-Gly-Ser-Val-Leu-Lys-Val-Ala-Ala-Lys-Val-Leu-Pro-Ala-Ala-Leu-Cys-Gln-Ile-Phe-Lys-Lys-Cys-OH

24

95.21%

C₁₂₃H₂₀₁N₂₉O₂₇S₂

2582.21

Synthetic

Powder

Brevinin-1LT2 is a novel antimicrobial peptide that was isolated from the skin secretion of the Chinese broad-folded frog, Hylarana latouchii. It belongs to the brevinin-1 family of antimicrobial peptides and has a high content of alpha-helix structure.
Brevinin-1LT2 is similar in structure and properties to another antimicrobial peptide called brevinin-1LT1, which was also isolated from the same frog species. Although the bioactivity of brevinin-1LT2 has not been determined, it is presumed to possess similar antimicrobial potency and specificity as brevinin-1LT1. Both brevinin-1LT1 and Brevinin-1LT2 kill microbes by disturbing their cell membranes, as observed through scanning electron microscopy (SEM) studies.

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

• Wang H, Yan X, Yu H, et al. Isolation, characterization and molecular cloning of new antimicrobial peptides belonging to the brevinin-1 and temporin families from the skin of Hylarana latouchii (Anura: Ranidae). Biochimie. 2009;91(4):540-7.

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.