β-Amyloid (11-22) peptide

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

Batch to batch variation of the purity

The Amyloid Beta (11-22) peptide, often denoted as Aβ_11–22, is a fragment derived from the full-length amyloid beta protein. This fragment encompasses the central hydrophobic core region of the parent peptide. Scientific studies indicate that the Aβ_11–22 fragment exhibits a distinct aggregation pathway characterized by the formation of long, extended, and twisted structures. This aggregation behavior is primarily driven by hydrophobic interactions inherent to its amino acid sequence.

Transmission electron microscopy analyses reveal that the Aβ_11–22 peptide forms these specific twisted morphologies, which are highly heterogeneous in length. Unlike the full-length amyloid beta peptide, the aggregation process and resulting structures of the Aβ_11–22 fragment are not significantly altered by the presence of certain exogenous metal complexes. The molecular organization of this fragment is determined by its specific sequence, contributing to the understanding of region-specific roles within the broader amyloid beta aggregation phenomenon.

• Cali MP, Pereira LMB, Teodoro MD, Sellani TA, Rodrigues EG, Carlos RM. Comparison of Aβ (1-40, 1-28, 11-22, and 29-40) aggregation processes and inhibition of toxic species generated in early stages of aggregation by a water-soluble ruthenium complex. J Inorg Biochem. 2021 Feb;215:111314. doi: 10.1016/j.jinorgbio.2020.111314. Epub 2020 Nov 21. PMID: 33261934.

Trifluoroacetic acid (TFA) is a common counterion from the purification process using High-Performance Liquid Chromatography (HPLC). The presence of TFA can affect the peptide's net weight, appearance, and solubility.

Impact on Net Weight: The TFA salt contributes to the total mass of the product. In most cases, the peptide content constitutes >80% of the total weight, with TFA accounting for the remainder.

Solubility: TFA salts generally enhance the solubility of peptides in aqueous solutions.

In Biological Assays: For most standard in vitro assays, the residual TFA levels do not cause interference. However, for highly sensitive cellular or biochemical studies, please be aware of its presence.