D-Cateslytin peptide

D-Cateslytin peptide

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

Batch to batch variation of the purity

RSMRLSFRARGYGFR (all D-type amino acids)

H-Arg-Ser-Met-Arg-Leu-Ser-Phe-Arg-Ala-Arg-Gly-Tyr-Gly-Phe-Arg-OH

15

95.2%

C₈₁H₁₃₀N₃₀O₁₉S₁

1860.18

Synthetic

Powder

The peptide cateslytin (RSMRLSFRARGYGFR) produced by enzymatic degradationof stress proteins is remarkably active against a large number of microorganisms including Plasmodium Falciparum responsible for Malaria. Its mode of action on membranes mimicking the external negatively charged membrane of these microorganisms has been studied by circular dichroism, infra-red (attenuatedtotal reflection), high-resolution magic angle sample spinning and wide line solid state NMR, patch clamp and molecular dynamics. The peptide, which is unstructuredin solution, adopts an aggregated beta sheet structure upon interacting with negatively charged membranes. D-Cateslytin (D-Ctl), a new epipeptide derived from L-Cateslytin, where all L-amino acids were replaced by D-amino acids. D-Ctl emerges as a potent, safe and robust peptide antimicrobial with undetectable susceptibility to resistance. Using Escherichia coli as a model, D-Ctl targets the bacterial cell wall leading to the permeabilization of the membrane and the death of the bacteria. Overall, D-Ctl offers many assets that make it an attractive candidate for the biopharmaceutical development of new antimicrobials either as a single therapy or as a combination therapy as D-Ctl also has the remarkable property to potentiate several antimicrobials of reference such as cefotaxime, amoxicillin and methicillin.

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

• Zaet A, Dartevelle P, Daouad F, et al. D-Cateslytin, a new antimicrobial peptide with therapeutic potential. Scientific Reports. 2017;7(1). doi:10.1038/s41598-017-15436-z.

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.