Peceleganan peptide

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

Batch to batch variation of the purity

Peceleganan is an α-helical antimicrobial peptide (AMP) characterized by its low molecular weight, amphipathic structure, and net positive charge. It exhibits broad-spectrum antibacterial activity against both Gram-positive and Gram-negative bacteria, with minimal inhibitory concentrations (MICs) ranging from 1 to 8 μM. The peptide's mechanism of action involves disrupting bacterial cell membranes, leading to increased permeability and loss of barrier function.

Peceleganan demonstrates functional synergy when combined with traditional antibiotics, enhancing their antibacterial efficacy. This synergy arises from the peptide's ability to compromise membrane integrity, facilitating antibiotic entry into bacterial cells. Its structural features, including hydrophobicity and charge distribution, contribute to its potent antimicrobial properties and selectivity for prokaryotic membranes.

• Feng Q, Huang Y, Chen M, Li G, Chen Y. Functional synergy of α-helical antimicrobial peptides and traditional antibiotics against Gram-negative and Gram-positive bacteria in vitro and in vivo. Eur J Clin Microbiol Infect Dis. 2015 Jan;34(1):197-204. doi: 10.1007/s10096-014-2219-3. Epub 2014 Aug 30. PMID: 25169965.

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.