Cys-KR12 peptide

Cys-KR12 peptide

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

Batch to batch variation of the purity

H-CKRIVKRIKKWLR-OH

H-Cys-Lys-Arg-Ile-Val-Lys-Arg-Ile-Lys-Lys-Trp-Leu-Arg-OH

13

95.51%

C₇₉H₁₄₃N₂₇O₁₄S

1727.21

Synthetic

Powder

Cys-KR12 peptide is a remarkable bioactive molecule with significant potential in the fields of wound care and infection prevention. Structurally, it features a cysteine residue at the N-terminus, followed by the sequence KRIVKRIKKWLR. This unique composition endows it with excellent antimicrobial properties, making it highly effective against a broad spectrum of bacteria, including both Gram-positive and Gram-negative strains such as Staphylococcus aureus, Staphylococcus epidermidis, Escherichia coli, and even methicillin-resistant Staphylococcus aureus (MRSA).
When immobilized on materials like starch-based sponges, Cys-KR12 peptide showcases its multifunctional capabilities. It not only provides inherent antimicrobial activity that can last for at least 5 days, but also contributes to the hemostatic function of the composite material. In the context of hemostatic sponges, Cys-KR12 peptide helps in reducing blood loss and shortening clotting time. It does so by promoting the adhesion and concentration of platelets and red blood cells at the bleeding site, facilitating the formation of a stable blood clot. This makes it an ideal candidate for the development of advanced wound dressings that can simultaneously address bleeding and the risk of infection, offering a more comprehensive solution for wound management.

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

• Yang X, Liu W, Xi G, Wang M, Liang B, Shi Y, Feng Y, Ren X, Shi C. Fabricating antimicrobial peptide-immobilized starch sponges for hemorrhage control and antibacterial treatment. Carbohydr Polym. 2019 Oct 15;222:115012. doi: 10.1016/j.carbpol.2019.115012. Epub 2019 Jun 20. PMID: 31320069.

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.