β- Amyloid (1-16) peptide

β- Amyloid (1-16) peptide

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

Batch to batch variation of the purity

DAEFRHDSGYEVHHQK

Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys

16

98%

C₈₄H₁₁₉N₂₇O₂₈

1955.05

131580-10-4

Synthetic

Powder

The Cu²⁺ complex of this soluble amyloid β-protein fragment showed significant oxidative activities toward the catechol-like substrate 1,2,3-trihydroxylbenzene (pyrogallol) and plasmid DNA cleavage. The N-terminal Aβ fragments Aβ1-14 (H-7372), Aβ1-15 (H-6368), and Aβ1-16 are elevated in cell media and in CSF in response to γ-secretase inhibitor treatment. The fragments can serve as biomarkers in clinical studies of the effect of such inhibitors.

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

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.