WRW4 peptide

WRW4 peptide

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

H-WRWWWW-NH2

H-Trp-Arg-Trp-Trp-Trp-Trp-NH2

6

95.85%

C₆₁H₆₅N₁₅O₆

1104.26

Synthetic

Powder

WRW4 is a selective antagonist of formyl peptide receptor 2 (FPR2) signaling, which can inhibit WKYMVm binding to FPR2 with an C50 of 0.23 μM and can also inhibit intracellular calcium release induced by WKYMVm, MMK 1, amyloid β42, and F peptide. WRW4 inhibits FPR2-mediated signaling in human neutrophils and blocks chemotactic migration and superoxide generation by amyloid β42 peptide. WRW4 can reduce Brucella proliferation in animal models.

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

• Bae et al (2004) Identification of peptides that antagonize formyl peptide receptor-like 1-mediating signaling. J.Immunol. 173 607 PMID: 15210823
• Kain et al (2018), Inhibition of FPR2 Impaired Leukocyte Get‐in Signal and Triggers Non‐Resolving Inflammation in Heart Failure. FASEB J. 32 287 PMID: 31216426
• Reyes et al (2021) Formyl peptide receptor 2 (FPR2) antagonism is a potential target for the prevention of Brucella abortus 544 infection, Immunobiology 226(3) 152073 https://doi.org/10.1016/j.imbio.2021.152073

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.