Px-cec1 peptide

Px-cec1 peptide

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

H-KPFKKLEKVGRNIRDGIIKAGPAVAVIGQATSIARPTGK-OH

H-Lys-Pro-Phe-Lys-Lys-Leu-Glu-Lys-Val-Gly-Arg-Asn-Ile-Arg-Asp-Gly-Ile-Ile-Lys-Ala-Gly-Pro-Ala-Val-Ala-Val-Ile-Gly-Gln-Ala-Thr-Ser-Ile-Ala-Arg-Pro-Thr-Gly-Lys-OH

39

95.15%

C₁₈₃H₃₁₈N₅₆O₄₉

4086.81

Synthetic

Powder

Px-cec1 is a cationic antibacterial peptide found in the diamondback moth, Plutella xylostella. It is encoded by a 480 bp full-length cDNA and is predominantly expressed in fat bodies, hemocytes, midgut, and epidermis, with the highest expression level in fat bodies.
Px-cec1 peptide exhibits a broad spectrum of antimicrobial properties against fungi, Gram-positive and Gram-negative bacteria, and does not exhibit hemolytic activity against human erythrocytes. The antibacterial activity of Px-cec1 is attributed to its ability to disrupt bacterial cell structures by acting on the cell membrane.
The recombinant Px-cec1 contains mainly alpha-helices and is stable over a wide range of pH values. It shows high activity against both Gram-negative and Gram-positive bacteria, as well as some fungi that can infect humans. The recombinant Px-cec1 can be produced using a thioredoxin fusion expression system in E. coli and purified using single-step affinity chromchromatography. The N-terminal two residues were altered to MA in the recombinant form.

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

• Jin F, Sun Q, Xu X, et al. cDNA cloning and characterization of the antibacterial peptide cecropin 1 from the diamondback moth, Plutella xylostella L. Protein Expr Purif. 2012;85(2):230-8.
• Ouyang L, Xu X, Freed S, Gao Y, Yu J, Wang S, Ju W, Zhang Y, Jin F. Cecropins from Plutella xylostella and Their Interaction with Metarhizium anisopliae. PLoS One. 2015 Nov 6;10(11):e0142451.

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.