Phyllokinin [T6,V10] sulphated peptide

Phyllokinin [T6,V10] sulphated peptide

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

H-RPPGFTPFRVY-OH

H-Arg-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg-Val-Tyr-OH

11

95.14%

C₆₅H₉₃N₁₇O₁₄

1336.53

Synthetic

Powder

The source of Phyllokinin [T6,V10] sulphated is tiger-legged waxy monkey tree frog / Southern orange-legged leaf frog (Phyllomedusa hypochondrialis azurea).
Phyllokinin [T6,V10] sulphated is a novel peptide that was identified in the skin secretions of Phyllomedusa hypochondrialis azurea. It is a variant of phyllokinin, a peptide that has been shown to be more potent than bradykinin on various preparations. The sulphation modification on the peptide appears to enhance its activity. It is one of the most abundant peptides found in the skin secretions of the frog species.

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

• Thompson AH, Bjourson AJ, Shaw C, Mcclean S. Bradykinin-related peptides from Phyllomedusa hypochondrialis azurea: Mass spectrometric structural characterisation and cloning of precursor cDNAs. Rapid Commun Mass Spectrom. 2006;20(24):3780-8.

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.