| Name
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Β-Amyloid (12-28)
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| Other Name
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|
| Sequence (Single letter abbreviations)
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VHHQKLVFFAEDVGSNK
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| Sequence（Three letter abbreviations）
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{Val}{His}{His}{Gln}{Lys}{Leu}{Val}{Phe}{Phe}{Ala}{Glu}{Asp}{Val}{Gly}{Ser}{Asn}{Lys}
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| Basic description
|
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 α-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.
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| The molecular weight
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1955.190
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| Chemical formula
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C89H135N25O25
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| The purity
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> 95%
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| Storage conditions
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Store β-amyloid (12-28) at -20°C.
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| Annotation
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| Documents
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| Figures
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| Reference
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Β-Amyloid (12-28)
