DWGKGGRWRLWPGASGKTEA - Inhibitorpeptid von Amyloid-beta

DWGKGGRWRLWPGASGKTEA peptide is one of several inhibitors of amyloid-beta aggregation that have been published. Many of them are fragments and modified peptides derived from the native amyloid-beta sequence. Others were identified by phage display approaches. An overview about peptides that target amyloid-beta is described by Stains et al. (2007) ChemMedChem 2, 1674-1692.

Characteristic of Alzheimer disease is the accumulation of amyloid plaques (amyloid-beta) in the brain. The major components of these plaques are 36-42 residue-long amyloid-beta-peptides, which form insoluble fibrils via self-assembly. 
The amyloid-beta-peptides are fragments of the broadly distributed, membrane-bound amyloid precursor protein APP, encoded on chromosome 21. They are formed from the proteolytic cleavage of APP by ß- and γ-secretases.
One of the most common and intensively studied amyloid ß isoforms is amyloid ß1-40), which is present in amyloid plaques. 

References:
M. Ahmed, J. Davis, D. Aucoin, T. Sato, S. Ahuja, S. Aimoto, J. I. Elliott, W. E. Van Nostrand, S. O. Smith (2010) Nat. Struct. Mol. Biol. 17, 561-567.
T. Hartmann, S. C. Bieger, B. Brühl, P. J. Tienari, N. Ida, D. Allsop, G. W. Roberts, C. L. Masters, C. G. Dotti, K. Unsicker, K. Beyreuther (1997) Nat. Med. 3, 1016-1020.

Amyloid-ß-peptides and innate immunity
In Alzheimer’s disease, deposition of amyloid-beta triggers a protracted sterile inflammatory response. Chronic stimulation of the innate immune system is believed to underlie the pathology of this disease. It was shown, that amyloid-beta triggers inflammatory signalling through a heterodimer of Toll-like receptors 4 and 6. Assembly of this recently identified heterodimer is regulated by signals from the scavenger receptor CD36, CD36-TLR4-TLR6 activation was identified as a common molecular mechanism by which atherogenic lipids and amyloid-beta stimulate sterile inflammation (Stewart et al. 2010, Nature Immunology 11, 155-161 doi:10.1038/ni.1836).

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