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Inside Cover: Introduction of d ‐Glutamate at a Critical Residue of Aβ42 Stabilizes a Prefibrillary Aggregate with Enhanced Toxicity (Chem. Eur. J. 34/2016)
Author(s) -
Warner Christopher J. A.,
Dutta Subrata,
Foley Alejandro R.,
Raskatov Jevgenij A.
Publication year - 2016
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201603417
Subject(s) - residue (chemistry) , toxicity , peptide , glutamate receptor , chemistry , cytotoxicity , amyloid beta , amino acid residue , amino acid , biochemistry , peptide sequence , organic chemistry , in vitro , receptor , gene
Learning by looking into a mirror , using a variant of the Alzheimer′s amyloid beta 42 peptide (E22e variant) with a d ‐amino acid introduced at the glutamate residue 22. Although low‐ n oligomers were unaffected, a soluble ordered intermediate unique to the E22e variant was identified, with a marked enhancement in the cytotoxicity against neuron‐like model cells. This study could help to deepen our understanding of the amyloid beta toxicity in Alzheimer′s disease. More information can be found in the Communication by J. A. Raskatov et al. on page 11967 ff.