Esculentin-2CHa peptide

Esculentin-2CHa peptide

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

H-GFSSIFRGVAKFASKGLGKDLAKLGVDLVACKISKQC-OH

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

37

95.46%

C₁₇₃H₂₈₉N₄₇O₄₇S₂

3843.54

Synthetic

Powder

Esculentin-2CHa is a peptide found in the skin secretions of Chiricahua leopard frog, Lithobates chiricahuensis, Arizona, USA, North America.
Esculentin-2Cha is a host-defense peptide with antimicrobial activity that exhibits potent growth inhibitory activity against multidrug-resistant strains of bacteria such as Staphylococcus aureus (MRSA), Acinetobacter baumannii, Stenotrophomonas maltophilia, E. coli, C. albicans, P. aeruginosa, and K. pneumoniae (MIC < 10 uM) and fungi C. albicans. It has shown potential as a therapeutically valuable anti-infective agent, particularly against multidrug-resistant Gram-negative bacteria.
Esculentin-2Cha is moderately hemolytic and cytotoxic, with a relatively low toxicity compared to other peptides. It shows differential cytotoxic activity against human erythrocytes and non-small cell lung adenocarcinoma A549 cells. The peptide stimulates the release of the anti-inflammatory cytokine IL-10 by mouse lymphoid cells and TNF-α production by peritoneal macrophages.
The hydrophobic N-terminal hexapeptide sequence of esculentin-2CHa is important for its growth inhibitory activity and cytotoxicity. Removal of the cyclic C-terminal domain and replacement of specific residues result in decreased cytotoxicity against microorganisms and mammalian cells. The primary structure of esculentin-2 has not been conserved between frog species, but the hydrophobic character of the N-terminal hexapeptide sequence has been maintained.

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

• Conlon JM, Mechkarska M, Coquet L, et al. Characterization of antimicrobial peptides in skin secretions from discrete populations of Lithobates chiricahuensis (Ranidae) from central and southern Arizona. Peptides. 2011;32(4):664-9.
• Attoub S, Mechkarska M, Sonnevend A, Radosavljevic G, Jovanovic I, Lukic ML, Conlon JM. Esculentin-2CHa: a host-defense peptide with differential cytotoxicity against bacteria, erythrocytes and tumor cells. Peptides. 2013 Jan;39:95-102.
• Ojo OO, Srinivasan DK, Owolabi BO, Vasu S, Conlon JM, Flatt PR, Abdel-Wahab YH. Esculentin-2CHa-Related Peptides Modulate Islet Cell Function and Improve Glucose Tolerance in Mice with Diet-Induced Obesity and Insulin Resistance. PLoS One. 2015 Oct 29;10(10):e0141549.
• Pantic JM, Jovanovic IP, Radosavljevic GD, Arsenijevic NN, Conlon JM, Lukic ML. The Potential of Frog Skin-Derived Peptides for Development into Therapeutically-Valuable Immunomodulatory Agents. Molecules. 2017 Dec 13;22(12):2071.
• Adesanoye OA, Farodoye OM, Adedara AO, Falobi AA, Abolaji AO, Ojo OO. Beneficial actions of esculentin-2CHa(GA30) on high sucrose-induced oxidative stress in Drosophila melanogaster. Food Chem Toxicol. 2021 Nov;157:112620.

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.