Esculentin-2ERa peptide

Esculentin-2ERa peptide

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

H-GLFSLFKAGAKILGKTFLKQAGKAGAEHLACKAANQC-OH

H-Gly-Leu-Phe-Ser-Leu-Phe-Lys-Ala-Gly-Ala-Lys-Ile-Leu-Gly-Lys-Thr-Phe-Leu-Lys-Gln-Ala-Gly-Lys-Ala-Gly-Ala-Glu-His-Leu-Ala-Cys-Lys-Ala-Ala-Asn-Gln-Cys-OH

37

95.43%

C₁₇₁H₂₈₀N₄₈O₄₅S₂

3792.46

Synthetic

Powder

Esculentin-2ERa is a peptide found in the skin secretions of the South-East Asian frog Hylarana erythraea. It belongs to the esculentin-2 family of antimicrobial peptides. Esculentin-2ERa peptide was first identified in the Eurasian frog Rana esculenta and has since been detected in the skins of several frog species, including H. erythraea.
The antimicrobial activity of esculentin-2ERa is effective against both Gram-positive and Gram-negative bacteria. However, its therapeutic potential is often limited by its high hemolytic activity against human erythrocytes.

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

• Al-ghaferi N, Kolodziejek J, Nowotny N, et al. Antimicrobial peptides from the skin secretions of the South-East Asian frog Hylarana erythraea (Ranidae). Peptides. 2010;31(4):548-54.

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.