H-Asp-Ala-His-Lys-OH peptide (TFA removed)

H-Asp-Ala-His-Lys-OH peptide (TFA removed)

• COA/MS/HPLC Report
• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

DAHK

H-Asp-Ala-His-Lys-OH

4

99.86%

C₁₉H₃₁N₇O₇

469.5

111543-77-2

Synthetic

Powder

The tetrapeptide DAHK corresponding to the N-terminal sequence of human serum albumin forms a tight binding site for Cu(II) ions. DAHK inhibits Cu(II)-induced oxidative DNA double strand breaks.The tetrapeptide is as effective as HSA in preventing neuronal death induced by CuCl2/ascorbic acid. DAHK may be an effective, small-molecular-weight alternative to HSA as a therapeutic agent for stroke.

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

• E.T.Gum et al., Stroke, 35, 590 (2004)

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.