(Des-Glu²²)-Amyloid β-Protein (1-40)

Description:

The mutant of Amyloid β is more resistant to degradation by two major Aβ-degrading enzymes, neprilysin and insulin-degrading enzyme. Synthetic mutant Aβ showed unusual aggregation properties with enhanced oligomerization but no fibrillization. It also inhibited hippocampal long-term potentiation more efficiently than wild-type Aβ.

Sequence:

DAEFRHDSGYEVHHQKLVFFADVGSNKGAIIGLMVGGVV

General

References

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Name	(Des-Glu²²)-Amyloid β-Protein (1-40)
Category	Beta-Amyloidand Related Peptides
One Letter Code	DAEFRHDSGYEVHHQKLVFFADVGSNKGAIIGLMVGGVV
Three Letter Code	{Asp}{Ala}{Glu}{Phe}{Arg}{His}{Asp}{Ser}{Gly}{Tyr}{Glu}{Val}{His}{His}{Gln}{Lys}{Leu}{Val}{Phe}{Phe}{Ala}{Asp}{Val}{Gly}{Ser}{Asn}{Lys}{Gly}{Ala}{Ile}{Ile}{Gly}{Leu}{Met}{Val}{Gly}{Gly}{Val}{Val}
Molecular Weight	4200.750
Application	Alzheimer's Disease

Kulic, L., et al. "Early accumulation of intracellular fibrillar oligomers and late congophilic amyloid angiopathy in mice expressing the Osaka intra-Aβ APP mutation." Translational psychiatry 2.11 (2012): e183-e183.

Umeda, Tomohiro, et al. "Hypercholesterolemia accelerates intraneuronal accumulation of Aβ oligomers resulting in memory impairment in Alzheimer's disease model mice." Life sciences 91.23-24 (2012): 1169-1176.

Ovchinnikova, Oxana Yu, et al. "The Osaka FAD mutation E22Δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity." Journal of molecular biology 408.4 (2011): 780-791.

Suzuki, Takayuki, et al. "E22Δ mutation in amyloid β-protein promotes β-sheet transformation, radical production, and synaptotoxicity, but not neurotoxicity." International Journal of Alzheimer’s Disease 2011 (2011).

Tomiyama, Takami, et al. "A new amyloid β variant favoring oligomerization in Alzheimer's‐type dementia." Annals of neurology 63.3 (2008): 377-387.