PE1 peptide

PE1 peptide

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

KIKFLKVLT

Lys-Ile-Lys-Phe-Leu-Lys-Val-Leu-Thr

9

95.4%

Synthetic

Powder

An N-terminal lipidated cyclic antibiotic with nonstandard amino acid Dab at positions 1, 3, and 6 (Warning: Dab, 2,4-diaminobutanoic acid, is two CH2 units less than lysine, although represented by K here in the sequence), D-amino acids for F4 and V7. The ring structure is proposed to occur between the C-terminal carboxylic and hydroxyl group of the N-terminal fatty acid portion. PE1 and PE2 share the same peptide backbone but have different fatty acid chains (C-end-OCHRCH2CO-N-end: R is C4H9 for PE1 and C3H7 for PE2). Because of the same amino acid sequence, PE1 and PE2 share this AP number. Both compounds are active against S. epidermidis CMCC 26069, S. aureus ATCC 25923, S. aureus ATCC 43300, E. coli ATCC 35318, E. coli 5539, P. aeruginosa ATCC 27853, P. aeruginosa 5215, and fungus C. albicans ATCC 10231 (MIC 1-8 ug/ml), better than polymyxin B in certain cases. The source of PE1 is Paenibacillus ehimensis B7.

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

• Huang Z, Hu Y, Shou L, Song M. Isolation and partial characterization of cyclic lipopeptide antibiotics produced by Paenibacillus ehimensis B7. BMC Microbiol. 2013;13:87.

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.