PR 39 peptide

PR 39 peptide

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

H-RRRPRPPYLPRPRPPPFFPPRLPPRIPPGFPPRFPPRFP-NH2

H-Arg-Arg-Arg-Pro-Arg-Pro-Pro-Tyr-Leu-Pro-Arg-Pro-Arg-Pro-Pro-Pro-Phe-Phe-Pro-Pro-Arg-Leu-Pro-Pro-Arg-Ile-Pro-Pro-Gly-Phe-Pro-Pro-Arg-Phe-Pro-Pro-Arg-Phe-Pro-NH2

39

95.25%

C₂₂₉H₃₄₆N₇₀O₄₀

4719.63

Synthetic

Powder

PR 39 is a 39 amino acid proline-rich cathelicidin host defence and immunomodulatory peptide isolated from porcine polymorphonuclear neutrophils. PR 39 plays a pivotal role in the innate immune defence of the pig against infections. Besides direct antimicrobial activity, PR 39 is involved in wound healing and also stimulates angiogenesis and inhibits inflammatory responses by selectively blocking proteasome degradation of IκBα.

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

• Li et al (2000) PR39, a peptide regulator of angiogenesis. Nat.Med. 6 356 PMID: 10613823
• Gaczynska et al (2003) Proline and arginine-rich peptides constitute a novel class of allosteric inhibitors of proteasome activity. Biochemistry 42 8663 PMID: 12873125
• Veldhuizen et al (2014) Antimicrobial and immunomodulatory activities of PR-39 derived peptides. PLoS One 9(4) e95939 PMID: 24755622

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.