Plantaricin NC8β peptide

Plantaricin NC8β peptide

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

Batch to batch variation of the purity

SVPTSVYTLGIKILWSAYKHRKTIEKSFNKGFYH

H-Ser-Val-Pro-Thr-Ser-Val-Tyr-Thr-Leu-Gly-Ile-Lys-Ile-Leu-Trp-Ser-Ala-Tyr-Lys-His-Arg-Lys-Thr-Ile-Glu-Lys-Ser-Phe-Asn-Lys-Gly-Phe-Tyr-His-COOH

34

95.2%

C₁₈₉H₂₈₉N₄₉O₄₇

3999.6

Synthetic

Powder

Bacteriocins are antimicrobial peptides that are produced by most microorganisms that contribute their defence mechanisms. PLNC8 α and PLNC8 β are class II bacteriocins. Both L- and D-PLNC8 αβ caused rapid disruption of lipid membrane integrity and were effective against both susceptible and antibiotic resistant strains. The D-enantiomer was stable against proteolytic degradation by trypsin compared to the L-enantiomer. Of the truncated peptides, β1–22, β7–34 and β1–20 retained an inhibitory activity. The peptides diffused rapidly (2 min) through the bacterial cell wall and permeabilized the cell membrane, causing swelling with a disorganized peptidoglycan layer. Interestingly, sub-MIC concentrations of PLNC8 αβ substantially enhanced the effects of different antibiotics in an additive or synergistic manner. PLNC8 αβ is active against Staphylococcus spp. and may be developed as adjuvant in combination therapy to potentiate the effects of antibiotics and reduce their overall use. PLNC8 α and β are short peptides, composed of 29 and 34 amino acids, respectively, and show structural stability against heat and pH. Both PLNC8 α and β are membrane active on their own, but whereas more than 5 μM of PLNC8 α was required to induce substantial perturbation of lipid bilayer integrity in a liposomal model system, less than 0.1 μM PLNC8 β caused the same effects.

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

• Bengtsson, T. et al. (2020) Plantaricin NC8 alpha-beta exerts potent antimicrobial activity against Staphylococcus spp. and enhances the effects of antibiotics. Scientific Reports. doi.org/10.1038/s41598-020-60570-w.

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.