OP-145 peptide

OP-145 peptide

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

Ac-IGKEFKRIVERIKRFLRELVRPLR-NH2

Ac-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Glu-Arg-Ile-Lys-Arg-Phe-Leu-Arg-Glu-Leu-Val-Arg-Pro-Leu-Arg-NH2

24

95.14%

C₁₄₂H₂₄₆N₄₆O₃₁

3093.75

Synthetic

Powder

OP-145 is a synthetic antimicrobial peptide derived from amino acid sequence 13–36 of human cathelicidin LL-37, further modified to favour the formation of an amphipathic helix. To improve stability against proteolytic degradation, the N-terminus is acetylated and the C-terminus amidated. OP-145 is a potent antibacterial, only lytic to human cells at high concentrations, and shows significant activity against nine methicillin-resistant Staphylococcus aureus (MRSA) strains, reducing their growth and biofilm formation. OP-145 is safe and effective against chronic middle ear infection (otitis media) in humans, and when formulated in poly(lactic-co-glycolic acid) (PLGA) microspheres, OP-145 exerts strong anti-biofilm effects on clinical isolated pathogens and exerts powerful anti-infection effects in vivo.

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

• Nell et al (2006) Development of novel LL-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application. Peptides 27(4):649 PMID: 16274847
• Malanovic et al (2015) Phospholipid-driven differences determine the action of the synthetic antimicrobial peptide OP-145 on Gram-positive bacterial and mammalian membrane model systems. Biochim Biophys Acta. 1848(10 Pt A) 2437 PMID: 26210299
• Ming and Huang (20217) The Antibacterial Effects of Antimicrobial Peptides OP-145 against Clinically Isolated Multi-Resistant Strains. Jpn J Infect Dis. 70(6) 601 PMID: 28890511
• Cheng et al (2022) The antimicrobial effects of PLGA microspheres containing the antimicrobial peptide OP-145 on clinically isolated pathogens in bone infections. Sci Rep. 12(1) 14541 PMID: 36008534

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.