Fibrinogen-Binding Inhibitor Peptide

Fibrinogen-Binding Inhibitor Peptide

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

Batch to batch variation of the purity

HHLGGAKQAGDV

H-His-His-Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val-OH

12

97.5%

C₅₀H₈₀N₁₈O₁₆

1189.3

89105-94-2

Synthetic

Powder

This synthetic dodecapeptide represents the specific platelet receptor recognition site of the human fibrinogen γ chain (residues 400-411). It is a potent inhibitor of the binding of fibrinogen, fibronectin, and von Willebrand factor to thrombin- or ADP-stimulated platelets. The peptide has also been used in studying phosphorylation processes associated with platelet activation.

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

• S.Timmons et al., Proc. Natl. Acad. Sci. USA, 81, 4935 (1984)
• E.F.Plow et al., J. Biol. Chem., 259, 5388 (1984)
• Z.M.Ruggeri et al., Proc. Natl. Acad. Sci. USA, 83, 5708 (1986)
• S.Williams and H.Gralnick, Thromb. Res., 46, 457 (1987)
• J.E.Ferrell, Jr. and G.S.Martin, Proc. Natl. Acad. Sci. USA, 86, 2234 (1989)
• R.R.Hantgan et al., Thromb. Haemost., 68, 694 (1992)

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.