Hymenochirin-1Pb peptide

Hymenochirin-1Pb peptide

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

Batch to batch variation of the purity

H-LKLSPETKDTLKKVLKGAIKGAIAIASLA-NH2

H-Leu-Lys-Leu-Ser-Pro-Glu-Thr-Lys-Asp-Thr-Leu-Lys-Lys-Val-Leu-Lys-Gly-Ala-Ile-Lys-Gly-Ala-Ile-Ala-Ile-Ala-Ser-Leu-Ala-NH2

29

95.15%

C₁₃₆H₂₄₆N₃₆O₃₇

2977.61

Synthetic

Powder

Hymenochirin-1Pb is a host-defense peptide isolated from the skin secretions of Merlin's clawed frog (Pseudhymenochirus merlini, Africa).
Hymenochirin-1Pb is structurally similar to hymenochirin-1B from Hymenochirus boettgeri and belongs to the hymenochirin-1P family.
Hymenochirin-1Pb is one of the 13 host-defense peptides identified in the skin secretions of P. merlini, which have antimicrobial activity against bacteria such as Staphylococcus aureus (MIC 5 uM) and Escherichia coli (MIC > 40 uM). The peptides from P. merlini, including Hymenochirin-1Pb, have been characterized for their structural and biological properties, and their potential as antimicrobial agents is being explored.

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, Prajeep M, Mechkarska M, et al. Characterization of the host-defense peptides from skin secretions of Merlin's clawed frog Pseudhymenochirus merlini: insights into phylogenetic relationships among the Pipidae. Comp Biochem Physiol Part D Genomics Proteomics. 2013;8(4):352-7.

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.