Antimicrobial peptide VGF[554-577]

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

Batch to batch variation of the purity

Antimicrobial peptide VGF[554-577] is a C-terminally amidated endogenous peptide derived from the neurosecretory protein VGF precursor. It was identified through electron transfer dissociation mass spectrometry analysis of secretory peptides from a human endocrine cell line. The peptide sequence contains multiple internal basic residues and undergoes extensive backbone fragmentation via ETD, enabling confident identification. Structural analysis indicates the presence of a prohormone convertase consensus motif at its C-terminal region, which includes a canonical amidation signal. The N-terminal 11 residues and the amidated C-terminus are implicated in its functional properties.

• Sasaki K., Osaki T., Minamino N.; "Large-scale identification of endogenous secretory peptides using electron transfer dissociation mass spectrometry."; Mol. Cell. Proteomics 12:700-709(2013).

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.