Tiger17 peptide

Tiger17 peptide

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

H-WCKPKPKPRCH-NH2

H-Trp-Cys-Lys-Pro-Lys-Pro-Lys-Pro-Arg-Cys-His-NH2

11

95.64%

C₆₂H₉₉N₂₁O₁₁S₂

1378.71

Synthetic

Powder

Tiger17 is an 11 amino acid peptide with a disulphide bridge between cysteines 2 and 10, which is a potent healer of skin wounds. Tiger17 was designed based on the antimicrobial peptides tigerinin-RC1 and tigerinin RC2, identified from the skin secretions of the crab eating frog Fejervarya cancrivora which also exert wound healing activity. Tiger17 exerts significant effects at various stages of wound healing progresses - the induction of macrophage recruitment to the wound site at the inflammatory reaction stage, the promotion of migration and proliferation of keratinocytes and fibroblasts, and at the tissue remodeling phase. In mouse models Tiger17 accelerates the healing of full-thickness wounds and promotes re-epithelialization of skin wounds.

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

• Tang et al (2014) A small peptide with potential ability to promote wound healing. PLoS One 9(3) e92082 PMID: 24647450
• Teixeira et al (2022) Tiger 17 and pexiganan as antimicrobial and hemostatic boosters of cellulose acetate-containing poly(vinyl alcohol) electrospun mats for potential wound care purposes. Int J Biol Macromol. 209 (Pt A) 1526 PMID: 35469947
• Teixeira et al (2022) Antibacterial and hemostatic capacities of cellulose nanocrystalline-reinforced poly(vinyl alcohol) electrospun mats doped with Tiger 17 and pexiganan peptides for prospective wound healing applications. Biomaterials Advances (137) 212830 https://doi.org/10.1016/j.bioadv.2022.212830

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.