IARR-Anal10 peptide

IARR-Anal10 peptide

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

H-IARRALKKAKRAAHKIPAAKKFARR-NH2

H-Ile-Ala-Arg-Arg-Ala-Leu-Lys-Lys-Ala-Lys-Arg-Ala-Ala-His-Lys-Ile-Pro-Ala-Ala-Lys-Lys-Phe-Ala-Arg-Arg-NH2

25

95.2%

C₁₂₈H₂₃₁N₄₉O₂₅

2856.51

Synthetic

Powder

AMPs have been studied as an alternative to conventional antibiotics. After the 97 amino acid protein BjAMP1 was isolated from B. japonicum, Peptide Cutter and CAMP were used to identify the mature AMP, mBjAMP1, composed of 21 amino acids, located at the C-terminus of BjAMP1. IARR-Anal10 is an analog of mBjAMP1, displayed not only the greatest antimicrobial and antibiofilm activities, but also no toxicity against human red blood cells or othermammalian cells. IARR-Anal10 had little or no effect on bacterial outer membrane permeability, membrane polarization or membrane integrity. Instead, it appears IARR-Anal10 binds bacterial DNA, as evidenced in DNA gel retardation assays. Thus, IARR-Anal10 likely kills bacteria through an intracellular mechanism. We also confirmed that IARR-Anal10 suppresses the virulence of K. pneumoniae to a degree similar to tigecycline, used to treat carbapenem-resistant Enterobacteriaceae infections. Notably, IARR-Anal10 did not induce development of resistance by K. pneumoniae, though both meropenem and tigecycline did so within a short time. IARR-Anal10 is a promising agent for treating infections caused by bacteria resistant to tigecycline and meropenem.

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

• Park J, Kang HK, Choi MC, et al. Antibacterial activity and mechanism of action of analogues derived from the antimicrobial peptide mBjAMP1 isolated from Branchiostoma japonicum. J Antimicrob Chemother. 2018;73(8):2054-2063

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.