Antibacterial peptide LL-37 amide, LL37 (TFA removed)

Antibacterial peptide LL-37 amide, LL37 (TFA removed)

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

Batch to batch variation of the purity

LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES-NH2

H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-NH2

37

97.75%

C₂₀₅H₃₄₁N₆₁O₅₂

4492.34

Synthetic

Powder

LL-37 is a 37-residue amphiphilic histidine-derived antimicrobial peptide with broad antimicrobial activity. LL-37 helps protect the cornea from infections and modulates wound healing, while exhibiting antibacterial and anti-biofilm activity against a variety of Gram-positive and Gram-negative human pathogens, and has wound-healing effects on the host. LL-37 is an antimicrobial peptide with angiogenic activity. It corresponds to amino acids 134-170 of the human cathelicidin antimicrobial protein hCAP18/LL-37 and is extracellularly released from hCAP18/LL-37 by proteolytic processing. hCAP18/LL-37 is an effector of the innate immune system and is expressed in leukocytes and epithelial cells where it is upregulated in association with inflammation and injury. An overexpression of hCAP18/LL-37 in a series of breast carcinomas could be demonstated

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

• S.Sandgren et al., J. Biol. Chem., 279, 17951 (2004)
• F.Neville et al., Biophys. J., 90, 1275 (2006)
• U.H.Durr et al., Biochim. Biophys. Acta, 1758, 1408 (2006)
• T.Tecle et al., Innate Immun., 16, 151 (2010)

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.