WLBU2 peptide

WLBU2 peptide

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

RRWVRRVRRWVRRVVRVVRRWVRR

Arg-Arg-Trp-Val-Arg-Arg-Val-Arg-Arg-Trp-Val-Arg-Arg-Val-Val-Arg-Val-Val-Arg-Arg-Trp-Val-Arg-Arg

24

95.83%

3400.12

Synthetic

Powder

This peptide was active at physiologic NaCl concentrations against S. aureus and mucoid and nonmucoid strains of P. aeruginosa (see the ref). It also kills three oral microorganisms (grown planktonically): S. gordonii, F. nucleatum, and P. gingivalis (Antimicrob Agents Chemother. 2007 May;51(5):1837-9). WLBU2 also reduced the bacterial burden of S. gordonii and F. nucleatum biofilms. The minimal DNA bundling concentrations of LL-37 and WLBU2 are similar to the concentrations necessary to ensure effective bacteria killing. CSA-13, a member of the ceragenin family, like natural LL37 or synthetic WLBU2 and HB71 peptides targets the bacterial wall through interactions with LPS and LTA. The ability of CSA-13 to maintain its bactericidal activity in the presence of negatively charged F-actin and DNA and the observed additive effect of CSA-13 with rhDNase I suggest that this synthetic antibiotic has potential advantages in treating chronic infection in CF airways (J Antimicrob Chemother. 2007 Sep;60(3):535-45). Animal model:mouse: For the mice given peptide post-bacterial infection, in the 1 mg/kg group, nine of nine animals died because of Pseudomonas sepsis; in the 3 mg/kg group, only one of nine succumbed to infection and in the 4 mg/kg group, all mice were protected (P < 0.0001) by the peptide (Deslouches B et al., 2007). 10/30/2010. The source of WLBU2 is De novo peptide design using only residues V, R, and W.

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

• Deslouches B, Phadke SM, Lazarevic V, et al. De novo generation of cationic antimicrobial peptides: influence of length and tryptophan substitution on antimicrobial activity. Antimicrob Agents Chemother. 2005;49(1):316-22.

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.