Cu-ATCUN type1 peptide

Cu-ATCUN type1 peptide

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

Batch to batch variation of the purity

H-GGHRRWKIVVIRWRR-NH2

H-Gly-Gly-His-Arg-Arg-Trp-Lys-Ile-Val-Val-Ile-Arg-Trp-Arg-Arg-NH2

15

95.2%

C₉₀H₁₄₈N₃₆O₁₅

1974.36

Synthetic

Powder

Antimicrobial peptides (AMPs) are short, amphipathic peptides that are typically cationic in sequence and display broad-spectrum activity against bacteria, fungi, and protists. Herein, we report the effect of appending the amino terminal copper and nickel binding motif (ATCUN) to Sub5. The Cu-ATCUN derivatives show a two- to three-fold increase in antimicrobial activity for a variety of microbes, relative to Sub5, with MICs as low as 0.3 ± 0.1 μM toward Enterococcus faecium. Sub5 and the ATCUN derivatives bind both plasmid DNA and 16s A-site rRNA with low micromolar affinity. Native Sub5 and the metallopeptide derivatives were shown to promote damage against DNA to similar extents in cellular studies against both Escherichia coli and Staphylococcus epidermidis, with an almost threefold higher activity against the latter organism. Liposome experiments show that the metallopeptides have a greater affinity for model membranes of E. coli and S. aureus relative to Sub5, which correlates with their enhanced antimicrobial activity. Sub5 and the metalloderivatives also display no cytotoxicity toward adult human dermal fibroblasts. Addition of the ATCUN motif conferred the ability to promote lipid oxidation toward E. coli and S. epidermidis and enhanced membrane permeability, as evidenced by the extent of ATP leaked from cellular membranes relative to Sub5 alone. These data suggest that Cu-ATCUN derivatives inhibit microbes through multiple modes of action, resulting in an enhancement in their overall potency.

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

• Alexander JL, Thompson Z, Yu Z, Cowan JA. Cu-ATCUN Derivatives of Sub5 Exhibit Enhanced Antimicrobial Activity via Multiple Modes of Action. ACS Chem Biol. 2019;14(3):449-458

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.