D-form of SLAY-P1 (D-P1) peptide

D-form of SLAY-P1 (D-P1) peptide

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

H-rlvrilvskrpvaikpyfrl-OH (D-form)

H-Arg-Leu-Val-Arg-Ile-Leu-Val-Ser-Lys-Arg-Pro-Val-Ala-Ile-Lys-Pro-Tyr-Phe-Arg-Leu-OH

20

95.2%

C₁₁₅H₁₉₈N₃₄O₂₃

2425.01

Synthetic

Powder

Decreasing the therapeutic pipeline for vancomycin-resistant Enterococci (VRE) calls for novel strategies to enhance our antibacterial arsenal. Herein, we investigated the potential applications of surface localized antimicrobial display (SLAY)-derived cationic peptides in the fight against VanA operon mediated vancomycin-resistant Enterococcus. Through determining their antibacterial spectrum, we found that SLAY peptide 1/2 displayed moderate bactericidal activity against Enterococcus with minimal inhibitory concentration (MIC) values of 2-8 μg/mL. Furthermore, we observed a significant synergistic activity between SLAY-P1 and vancomycin against VRE. Mechanistic studies demonstrated that SLAY-P1 specifically inhibits transcription of the vanRS two-component system, thereby restoring vancomycin activity and resulting in the accumulation of the cell wall precursor. Meaningfully, the combination of SLAY-P1 and vancomycin prevents the emergence of vancomycin resistance. Consistent with in vitro synergistic results, the addition of SLAY-P1 significantly enhanced the survival rates of Galleria mellonella larvae compared with vancomycin monotherapy. Taken together, these results suggested that SLAY-derived cationic peptides not only display antibacterial activity against VRE but also reverse vancomycin resistance in Enterococcus, providing promising candidates for combating vancomycin-resistant pathogens.

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

• Liu Y, Jia Y, Yang K, Li R, Xiao X, Wang Z. Antagonizing Vancomycin Resistance in Enterococcus by Surface Localized Antimicrobial Display-Derived Peptides. ACS Infect Dis. 2020;6(5):761-767. doi:10.1021/acsinfecdis.9b00164

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.