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Beta - Amyloid (1 - 28)
| Overview | |
|---|---|
| Description | The three-dimensional solution structure of Aß (1-28) reveals the folding of the peptide to form a predominantly a-helical structure with a bend centered at residue 12 and the side chains of histidine-13 and lysine-16 in close proximity, residing on the same face of the helix. Their proximity may constitute a binding motif with the heparan sulfate proteoglycans. Aß (1-28) is highly hydrophilic and shares sequences with bA4, the major component of Aß. Its assembly is fibrillar, i.e., elongated in a single direction. Reports show that synthetic peptides Aß (1-40) and Aß (1-28) have significant effects on normal human plasma cholesterol esterification rate. Both peptides (at concentration of 1 ng/mL) inhibit plasma cholesterol esterification rate by 40-50% compared to the control value. |
| Sequence | DAEFRHDSGYEVHHQKLVFFAEDVGSNK |
| Sequence (3 Letter) | H-Asp-Ala-Glu-Phe-Arg-His-Asp-Ser-Gly-Tyr-Glu-Val-His-His-Gln-Lys-Leu-Val-Phe-Phe-Ala-Glu-Asp-Val-Gly-Ser-Asn-Lys-OH |
| Molecular Weight | 3262.5 |
| Properties | |
| Purity | > 95% By HPLC |
| Storage | Store at -20 °C, cap vial tightly at all times. |
Kirshenbaum K. and V. Daggett, Biochem. 34, 7640 (1995); Talafous, J. et al. Biochem. 33, 7788 (1994).
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