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A peptide derived from Abeta17-36 crystallizes to form trimers that further associate to form higher-order oligomers. The trimers consist of three highly twisted beta-hairpins in a triangular arrangement. Two trimers associate face-to-face in the crystal lattice to form a hexamer; four trimers in a tetrahedral arrangement about a central cavity form a dodecamer. These structures provide a working model for the structures of oligomers associated with neurodegeneration in Alzheimer's disease.
X-ray Crystallographic Structures of Trimers and Higher-Order Oligomeric Assemblies of a Peptide Derived from Abeta,Spencer RK, Li H, Nowick JS J Am Chem Soc. 2014 Apr 3. PMID:24669800[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Spencer RK, Li H, Nowick JS. X-ray Crystallographic Structures of Trimers and Higher-Order Oligomeric Assemblies of a Peptide Derived from Abeta J Am Chem Soc. 2014 Apr 3. PMID:24669800 doi:http://dx.doi.org/10.1021/ja5017409
