LFB peptide

LFB peptide

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

H-GLFSVVKGVLKGVGKNVSGSLLDQLKCKISGGC-OH

H-Gly-Leu-Phe-Ser-Val-Val-Lys-Gly-Val-Leu-Lys-Gly-Val-Gly-Lys-Asn-Val-Ser-Gly-Ser-Leu-Leu-Asp-Gln-Leu-Lys-Cys-Lys-Ile-Ser-Gly-Gly-Cys-OH

33

95.2%

C₁₄₅H₂₅₂N₄₀O₄₂S₂

3291.91

Synthetic

Powder

LFB is a novel antimicrobial brevinin-like peptide from the skin secretion of the fujian large headed frog, Limnonectes fujianensi. LFB belongs to the Brevinin family and its structural conformation reflects the presence of three basic characteristic physico-chemical attributes: alpha-helix, beta-sheet and random coil. LFB displayed notable potency against the Gram positive bacterium S. aureus, the Gram negative bacterium E. coli and the yeast C. albicans. Furthermore, LFB could also inhibit the growth of human cancer cell lines, with IC50 values ranging from 18.9uM down to 2.0uM.

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 B, Lyu P, Xie S, et al. LFB: A Novel Antimicrobial Brevinin-Like Peptide from the Skin Secretion of the Fujian Large Headed Frog, Limnonectes fujianensi. Biomolecules. 2019;9(6)

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.