Variegin [E31] peptide

Variegin [E31] peptide

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

H-SDQGDVAEPKMHKTAPPFDFEAIPEEYLDDES-OH

H-Ser-Asp-Gln-Gly-Asp-Val-Ala-Glu-Pro-Lys-Met-His-Lys-Thr-Ala-Pro-Pro-Phe-Asp-Phe-Glu-Ala-Ile-Pro-Glu-Glu-Tyr-Leu-Asp-Asp-Glu-Ser-OH

32

95.36%

C₁₅₈H₂₃₁N₃₇O₅₈S

3608.78

Synthetic

Powder

Variegin is a novel thrombin inhibitor found in the salivary gland extract of the tropical bont tick, Amblyomma variegatum. It is one of the smallest thrombin inhibitors known. Variegin binds to thrombin with strong affinity (K i ≈ 10.4 pM) and high specificity. The N-terminus of variegin affects the binding kinetics, with the removal of the seven residues leading to a change from fast to slow binding. The active site binding moiety of variegin is located in residues 8-14, while the exosite-I binding moiety is within residues 15-32. Variegin is structurally and functionally similar to the rationally designed thrombin inhibitor, hirulog, but it is a more potent inhibitor and retains its inhibitory activity even after cleavage by thrombin. Variegin provides a promising platform for the development of new thrombin inhibitors.
Variegin [E31] has the complete sequence of variegin without seven-residues removal on the N-terminal, so it is the version of Variegin with the fastest binding kinetic.

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

• Koh CY, Kazimirova M, Trimnell A, et al. Variegin, a novel fast and tight binding thrombin inhibitor from the tropical bont tick. J Biol Chem. 2007;282(40):29101-13.

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.