Entericidin A peptide

Entericidin A peptide

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

H-CNTARGFGEDIKHLGNSISHAAS-OH

H-Cys-Asn-Thr-Ala-Arg-Gly-Phe-Gly-Glu-Asp-Ile-Lys-His-Leu-Gly-Asn-Ser-Ile-Ser-His-Ala-Ala-Ser-OH

23

95.71%

C₉₉H₁₅₇N₃₃O₃₄S

2385.56

Synthetic

Powder

Entericidin A is a protein encoded by the entericidin locus in Escherichia coli and Citrobacter freundii. It is a small cell-envelope lipoprotein that acts as an antidote to the bacteriolytic lipoprotein entericidin B. The entericidin locus is activated in stationary phase under high osmolarity conditions and is regulated by the osmoregulatory EnvZ/OmpR signal transduction pathway. The Entericidin A lipoprotein is predicted to adopt an amphipathic α-helical structure and is involved in modulating membrane stability. The entericidin locus is conserved in the homologous region of the Citrobacter freundii chromosome. The organization of the entericidin locus as a chromosomal antidote/toxin gene pair, regulated by both positive and negative osmotic signals during starvation, suggests its involvement in programmed bacterial cell death.

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

• Bishop RE, Leskiw BK, Hodges RS, Kay CM, Weiner JH. The entericidin locus of Escherichia coli and its implications for programmed bacterial cell death. J Mol Biol. 1998;280(4):583-96.

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.