α-Synuclein (61-95) (human)

Description:

Accumulation of α-synuclein (61-95) aggregates in the synapse might be responsible for the neurodegeneration in AD and in the prion diseases. The α-synuclein (61-95) has originally been isolated from the insoluble core of Alzheimer's disease amyloid plaque.

Sequence:

EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFV

General

References

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Name	α-Synuclein (61-95) (human)
Category	Beta-Amyloidand Related Peptides
One Letter Code	EQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFV
Three Letter Code	{Glu}{Gln}{Val}{Thr}{Asn}{Val}{Gly}{Gly}{Ala}{Val}{Val}{Thr}{Gly}{Val}{Thr}{Ala}{Val}{Ala}{Gln}{Lys}{Thr}{Val}{Glu}{Gly}{Ala}{Gly}{Ser}{Ile}{Ala}{Ala}{Ala}{Thr}{Gly}{Phe}{Val}
Molecular Weight	3260.650
Application	Alzheimer's DiseaseParkinson's Disease

Söderberg, Linda, et al. "Characterization of the Alzheimer's disease-associated CLAC protein and identification of an amyloid β-peptide-binding site." Journal of Biological Chemistry 280.2 (2005): 1007-1015.

Lotz, Miriam, et al. "Amyloid beta peptide 1–40 enhances the action of Toll‐like receptor‐2 and‐4 agonists but antagonizes Toll‐like receptor‐9‐induced inflammation in primary mouse microglial cell cultures." Journal of neurochemistry 94.2 (2005): 289-298.

Bodles, Angela M., et al. "Identification of the region of non‐Aβ component (NAC) of Alzheimer's disease amyloid responsible for its aggregation and toxicity." Journal of neurochemistry 78.2 (2001): 384-395.

Bodles, Angela M., et al. "Toxicity of non‐Aβ component of Alzheimer's disease amyloid, and N‐terminal fragments thereof, correlates to formation of β‐sheet structure and fibrils." European journal of biochemistry 267.8 (2000): 2186-2194.

Kakimura, J. "Kitamura Y, Takata K, Umeki M, Suzuki S, Shibagaki K, Taniguchi T, Nomura Y, Gebicke-Haerter PJ, Smith MA, Perry G, and Shimohama S." Microglial activation and amyloid-β clearance induced by exogenous heat-shock proteins. FASEB J 16 (2002): 601-603.