Jelleine-I peptide (TFA removed)

Jelleine-I peptide (TFA removed)

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

Batch to batch variation of the purity

PFKLSLHL-NH2

Pro-Phe-Lys-Leu-Ser-Leu-His-Leu-NH2

8

97.63%

C₄₇H₇₆N₁₂O₉

953.24

Synthetic

Powder

Active against G+ bacteria S. aureus ATCC 6535, S. saprophyticus, B. subtilis CCT 2471 (MIC 10-15 ug/ml), and G- bacteria E. coli CCT 1371 (MIC 2.5 ug/ml), E. cloacae ACCT 23355, K. pneumoniae ACCT 13883, P. aeruginsa ACCT 27853 (MIC 10 ug/ml), and yeast C. albicans (MIC 2.5 ug/ml). Jelleines are produced constitutively by the workers and secreted into Royal Jelly. This peptide can show synergistic killing of Gram-positive bacteria with temporin A or B (Romanelli A et al 2011 Peptides Jan 19. doi: 10.1002/psc.1316). Updated Jan 2011; 7/2014. Jelleine-I has Antibacterial, Antifungal activity. The source of Jelleine-I is honeybees, Apis mellifera.

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

• Fontana R, Mendes MA, De souza BM, et al. Jelleines: a family of antimicrobial peptides from the Royal Jelly of honeybees (Apis mellifera). Peptides. 2004;25(6):919-28.

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.