Fraternine peptide

Fraternine peptide

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

H-LSFQQVKEKVCKVEAKIGKKLPFC-NH2

H-Leu-Ser-Phe-Gln-Gln-Val-Lys-Glu-Lys-Val-Cys-Lys-Val-Glu-Ala-Lys-Ile-Gly-Lys-Lys-Leu-Pro-Phe-Cys-NH2, disulfide bond forms between Cys11 and Cys24

24

95.2%

C₁₂₆H₂₁₁N₃₃O₃₁S₂

2748.34

Synthetic

Powder

Fraternine, a Novel Wasp Peptide, Protects against Motor Impairments in 6-OHDA Model of Parkinsonism. This peptide protected against some of the motor alterations and neuronal death in a 6-OHDA model of parkinsonism. The primary sequence of Fraternine showed a high percentage of identity (75%) with the peptide Sylverin isolated from the venom of the Protonectarina sylveirae wasp. Fraternine induced a dose-dependent antiparkinsonian effect in the Rotarod test. Fraternine does not cause motor alterations.

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

• Biolchi AM, de Oliveira DGR, Amaral HO, Campos GAA, Gonu00e7alves JC, de Souza ACB, et al. Fraternine, a Novel Wasp Peptide, Protects against Motor Impairments in 6-OHDA Model of Parkinsonism. Toxins (Basel). 2020;12(9)

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.