[Pyr11]-beta-Amyloid (11-40) – 1 mg

[Pyr11]-beta-Amyloid (11–40) – 1 mg is a synthetic peptide fragment derived from the amyloid-beta (Aβ) protein, specifically representing amino acids 11 through 40 with a pyroglutamate (Pyr) modification at position 11. Amyloid-beta peptides are cleavage products of the amyloid precursor protein (APP) and are widely studied in neuroscience research, particularly in relation to protein aggregation and neurodegenerative disease mechanisms. The pyroglutamate modification increases hydrophobicity and structural stability, which can influence aggregation behavior compared to non-modified Aβ fragments.

The (11–40) fragment differs from the full-length Aβ1-40 or Aβ1-42 peptides because it lacks the N-terminal residues 1–10. This truncation, combined with the pyroglutamate modification, alters its biochemical characteristics. Pyroglutamate-modified amyloid peptides are known in research literature to demonstrate enhanced resistance to enzymatic degradation and a higher tendency to form oligomers and fibrils. These structural features make [Pyr11]-Aβ (11–40) a valuable tool in laboratory studies focused on aggregation kinetics, peptide stability, and toxicity modeling.

In research settings, a 1 mg quantity is typically supplied as a lyophilized (freeze-dried) powder to maintain stability during storage and transport. Scientists reconstitute the peptide using appropriate laboratory-grade solvents depending on experimental requirements, such as aggregation assays, cell culture models, or biophysical analyses like circular dichroism or electron microscopy. Proper handling under controlled laboratory conditions is essential to maintain peptide integrity and reproducibility of results.

This peptide is primarilyThis peptide is primarily used for in vitro and in vivo experimental research to better understand amyloid formation pathways and to evaluate potential therapeutic strategies targeting modified amyloid species. Pyroglutamate forms of amyloid-beta have been investigated for their potential role in accelerating plaque formation and influencing neurotoxicity. As such, [Pyr11]-Aβ (11–40) helps researchers explore how post-translational modifications impact disease progression mechanisms at the molecular level.

It is important to note that [Pyr11]-beta-Amyloid (11–40) is strictly intended for laboratory research use only. It is not approved for human consumption, therapeutic application, or diagnostic use outside of controlled scientific studies. Proper storage—typically at low temperatures and protected from moisture—ensures peptide stability and preserves experimental reliability.