Px-Moricin peptide

Px-Moricin peptide

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

Batch to batch variation of the purity

H-APKVNVNALKKGGRVIKKGLGVIGAAGTAHEVYNHVRNRNQG-NH2

H-Ala-Pro-Lys-Val-Asn-Val-Asn-Ala-Leu-Lys-Lys-Gly-Gly-Arg-Val-Ile-Lys-Lys-Gly-Leu-Gly-Val-Ile-Gly-Ala-Ala-Gly-Thr-Ala-His-Glu-Val-Tyr-Asn-His-Val-Arg-Asn-Arg-Asn-Gln-Gly-NH2

42

95.2%

C₁₉₁H₃₂₅N₆₇O₅₂

4392.02

Synthetic

Powder

Px-Moricin is a novel AMP moricin from diamondback moth (Plutella xylostella). Px-Mor exhibited a broad antimicrobial spectrum against Gram positive bacteria (GPB), Gram negative bacteria (GNB) and fungi. Moreover, scanning electron microscopy and transmission electron microscopy (TEM) revealed that Px-Mor can cause obvious morphological alterations in A. pullulans, which demonstrated its powerful effect on the mycelia growth inhibition. The relative expression levels of Px-Mor were highest in fourth instar and prepupa stage, suggesting that moricin played different roles at different developmental stages. Px-Mor may be mainly expressed in changeable period of metamorphosis of prepupa development, which illustrated that Moricin have certain biological significance during the process of metamorphosis.

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

• Xu X, Zhong A, Wang Y, et al. Molecular Identification of a Moricin Family Antimicrobial Peptide (Px-Mor) From Plutella xylostella With Activities Against the Opportunistic Human Pathogen Aureobasidium pullulans. Front Microbiol. 2019

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.