Bacteriocin, Plantaricin A peptide

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

Batch to batch variation of the purity

Plantaricin A is a bacteriocin produced by Lactobacillus plantarum C11. It is a member of the nonlantibiotic class of bacteriocins, characterized by small peptide size, high isoelectric point, and the absence of post-translationally modified amino acids like lanthionine. Maximum bacteriocin activity is associated with the complementary action of two nearly identical peptides, α and β, which are derived from a 48-amino acid precursor encoded by the plnA gene. The mature peptides are generated by proteolytic cleavage of the precursor, a process common among nonlantibiotic bacteriocins.

The structural gene for plantaricin A, plnA, is located on a chromosomal operon that includes three additional open reading frames: plnB, plnC, and plnD. These genes are cotranscribed on a 3.3-kb mRNA transcript. The products of plnB, plnC, and plnD show strong homology to components of bacterial two-component signal transduction systems, particularly the accessory gene regulatory (agr) system of Staphylococcus aureus. This genetic organization suggests that the production or function of plantaricin A may be linked to the regulatory activity of this adjacent two-component system.

• Diep DB, Håvarstein LS, Nissen-meyer J, Nes IF. The gene encoding plantaricin A, a bacteriocin from Lactobacillus plantarum C11, is located on the same transcription unit as an agr-like regulatory system. Appl Environ Microbiol. 1994;60(1):160-6.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.