Ponericin-Q42 (insects, arthropods, invertebrates, animals, UCLL1a) peptide

Ponericin-Q42 (insects, arthropods, invertebrates, animals, UCLL1a) peptide

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

H-FWGAVWKILSKVLPHIPGTVKWLQEKV-OH

H-Phe-Trp-Gly-Ala-Val-Trp-Lys-Ile-Leu-Ser-Lys-Val-Leu-Pro-His-Ile-Pro-Gly-Thr-Val-Lys-Trp-Leu-Gln-Glu-Lys-Val-OH

27

95.69%

C₁₅₆H₂₃₉N₃₇O₃₃

3160.78

Synthetic

Powder

Ponericin-Q42 is a linear antimicrobial peptide isolated from the venom of the ant species Ectatomma quadridens. It is one of three peptides with low similarity to the well-known ponericin peptides found in the ant venom.
The peptide has a partially helical secondary structure, even in aqueous environments, which is unusual for short linear peptides.
Ponericin-Q42 has been shown to possess marked antibacterial activity against both Gram-positive and Gram-negative bacteria at low micromolar concentrations. For example, it is active against A. globiformis VKM Ac-1112, B. subtilis VKM B-501, E. coli MH1 (MIC 0.2-0.6 uM), E. coli DH5a, and P. aeruginosa PAO1 (MIC 5-10 uM). It also exhibits broad-spectrum cytolytic activity against different bacterial strains, human erythrocytes, and chronic myelogenous leukemia K562 cells. Ponericin-Q42 also has weak toxic activity on flesh fly larvae, with an LD50 of approximately 105 mg/g.

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

• Pluzhnikov KA, Kozlov SA, Vassilevski AA, Vorontsova OV, Feofanov AV, Grishin EV. Linear antimicrobial peptides from Ectatomma quadridens ant venom. Biochimie. 2014;107 Pt B:211-5.
• Kozic M, Fox SJ, Thomas JM, Verma CS, Rigden DJ. Large scale ab initio modeling of structurally uncharacterized antimicrobial peptides reveals known and novel folds. Proteins. 2018 May;86(5):548-565.

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.