RW2 peptide

RW2 peptide

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

Batch to batch variation of the purity

H-RWRW-NH2

H-Arg-Trp-Arg-Trp-NH2

4

95.32%

C₃₄H₄₇N₁₃O₄

701.82

Synthetic

Powder

RW2 is a short peptide containing repeating arginine (R) and tryptophan (W) residues which has been shown to possess antimicrobial and antifungal activity with low cytotoxicity. The positively charged arginine interacts with the bacterial membrane through electrostatic attraction whereas the non-polar tryptophan residue interacts with the lipid bilayer. These two properties allow RW2 to interact with the bacterial membrane, resulting in membrane destabilization and pore formation and bacterial cell death. RW2 has been shown to have enhanced activity in combination with other antimicrobial agents.

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

• Strøm et al (2002) Antimicrobial activity of short arginine- and tryptophan-rich peptides. J. Pept. Sci. 8(8) 431 PMID: 12212806
• Liu et al (2007) Length effects in antimicrobial peptides of the (RW)n series. Antimicrob. Agents Chemother. 51(2) 597 PMID: 17145799
• Mohan et al (2014) Enhanced antimicrobial activity of peptide-cocktails against common bacterial contaminants of ex vivo stored platelets. Clin. Microbiol. Infect. 20(1) O39 PMID: 23926880

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.