Amyloid beta (Abeta) (AA 12-28) Peptide
-
- Target See all beta Amyloid (Abeta) products
- beta Amyloid (Abeta) (Amyloid beta (Abeta))
- Protein Region
- AA 12-28
- Purity
- 95 %
-
-
- Restrictions
- For Research Use only
-
- Storage
- -20 °C
-
- Target
- beta Amyloid (Abeta) (Amyloid beta (Abeta))
- Synonyms
- AAA Peptide, ABETA Peptide, ABPP Peptide, AD1 Peptide, APPI Peptide, CTFgamma Peptide, CVAP Peptide, PN-II Peptide, PN2 Peptide, aaa Peptide, abeta Peptide, abpp Peptide, ad1 Peptide, appi Peptide, ctfgamma Peptide, cvap Peptide, pn2 Peptide, Abeta Peptide, Abpp Peptide, Adap Peptide, Ag Peptide, Cvap Peptide, E030013M08Rik Peptide, betaApp Peptide, amyloid beta precursor protein Peptide, amyloid beta (A4) precursor protein Peptide, APP Peptide, app Peptide, App Peptide
- Background
- Aß (12–28) residues are the binding site for apolipoprotein E (apoE) on Aß. This sequence encompasses a hydrophobic domain (residues 14–21) and a ß-turn (residues 22–28) which place two hydrophobic domains of Aß 14 to 21 and 29 to 40/42 opposite each other, allowing for the assembly of Aß peptides into fibrils. The secondary structure of Aß (12- 28), a neutral peptide, is dominated by --helix and random coil. The interaction of apoE with residues 12 to 28 of Aß is not just a non-specific hydrophobic interaction but plays a pivotal role in the mechanism of Aß pathology in Alzheimer’s disease (AD). Beta-amyloid (12-28) and five other fragments enhanced aggregation of full length Aß (1-40). All of the peptides that enhance aggregation contained either residues 17 to 20 or 30 to 35, indicating the importance of these regions for promoting aggregation of full-length Aß.
-