KCF18 peptide (TFA removed)

KCF18 peptide (TFA removed)

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

Batch to batch variation of the purity

H-KCRKEMFKQKLPYSTVYF-OH

H-Lys-Cys-Arg-Lys-Glu-Met-Phe-Lys-Gln-Lys-Leu-Pro-Tyr-Ser-Thr-Val-Tyr-Phe-OH

18

95.95%

C₁₀₇H₁₆₆N₂₆O₂₆S₂

2296.74

Synthetic

Powder

KCF18 exhibits amphiphilic properties, characterized by its positively charged and hydrophobic residues, which make it a strong candidate for inhibiting cytokine-induced inflammatory responses. Simulations revealed that KCF18 can simultaneously bind to cytokines, primarily through electrostatic interactions. Experiments involving surface plasmon resonance detection and MM/PBSA binding free energy calculations confirmed KCF18's ability to bind to both tumor necrosis factor-α (TNF-α) and interleukin-6. In cellular experiments, KCF18 effectively reduced the binding of proinflammatory cytokines to their specific receptors, suppressed TNF-α mRNA expression, and inhibited monocyte binding and transmigration. Additionally, in a mouse model of peritonitis, KCF18 decreased white blood cell infiltration. By diminishing plasma cytokine release and directly affecting the vascular endothelium, KCF18 shows promise in lowering the risk of vascular inflammation. This study underscores the potential of integrating structure-based in silico design with experimental methods to develop new anti-inflammatory agents.

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

• Jiang SJ, Tsai PI, Peng SY, Chang CC, Chung Y, Tsao HH, Huang HT, Chen SY, Hsu HJ. A potential peptide derived from cytokine receptors can bind proinflammatory cytokines as a therapeutic strategy for anti-inflammation. Sci Rep. 2019 Feb 19;9(1):2317. doi: 10.1038/s41598-018-36492-z. PMID: 30783144; PMCID: PMC6381106.
• Chang CC, Peng SY, Tsao HH, Huang HT, Lai XY, Hsu HJ, Jiang SJ. A Multitarget Therapeutic Peptide Derived From Cytokine Receptors Based on in Silico Analysis Alleviates Cytokine-Stimulated Inflammation. Front Pharmacol. 2022 Mar 10;13:853818. doi: 10.3389/fphar.2022.853818. PMID: 35370629; PMCID: PMC8965626.

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.