Antimicrobial peptide zp37

Antimicrobial peptide zp37

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

Batch to batch variation of the purity

H-GIKAKIIIKIKK-NH2

H-Gly-Ile-Lys-Ala-Lys-Ile-Ile-Ile-Lys-Ile-Lys-Lys-NH2

12

95.2%

C₆₅H₁₂₆N₁₈O₁₂

1351.8

Synthetic

Powder

The antimicrobial peptide zp37 (GIKAKIIIKIKK-NH2), which possesses a helical structure, was found to exhibit a minimum inhibitory concentration (MIC) value of 16 μM on E. coli O157:H7, effectively killing such strain in vitro and reducing its population size by 94.7% in sprouts upon storage for seven days. In sprouts, zp37 treatment reduced 94.7% E. coli O157:H7 upon storage for 7 days. zp37 caused membrane depolarization and weak membrane permeabilization. zp37 bound to the DNA of E. coli O157:H7, causing DNA aggregation and precipitation.

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

• Lanhua Yi, Ping Zeng, Jun Liu, Kwok-Yin Wong, Edward Wai-Chi Chan, Yanbing Lin, Kin-Fai Chan, Sheng Chen. Antimicrobial peptide zp37 inhibits Escherichia coli O157:H7 in alfalfa sprouts by inflicting damage in cell membrane and binding to DNA, LWT, Volume 146, 2021, 111392, ISSN 0023-6438

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.