Amyloid β-Protein (29-40) peptide

Amyloid β-Protein (29-40) peptide

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

GAIIGLMVGGVV

Gly-Ala-Ile-Ile-Gly-Leu-Met-Val-Gly-Gly-Val-Val

12

96.3%

C₄₉H₈₈N₁₂O₁₃S

1085.4

Synthetic

Powder

Aβ 29-40, a C-terminal fragment of predominant Aβ 1-40, has physicochemical properties related to those of the fusion peptides of viral proteins. Aβ 29-40 can induce the fusion of liposomes in vitro. The apoE2 and apoE3 apolipoprotein isoforms are potent inhibitors of the fusogenic and aggregational properties of this peptide. Reciprocally this amyloid β-peptide interacts with apoE2 and apoE3 and decreases or disturbs their normal association with lipids. This domain of the amyloid β-protein could be critical for the amyloid-apoE interaction.

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.