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Front Cover: Cu II Binding to Various Forms of Amyloid‐β Peptides: Are They Friends or Foes? (Eur. J. Inorg. Chem. 1/2018)
Author(s) -
Borghesani Valentina,
Alies Bruno,
Hureau Christelle
Publication year - 2018
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201701373
Subject(s) - chemistry , front cover , cover (algebra) , peptide , amyloid (mycology) , stereochemistry , biochemistry , biophysics , inorganic chemistry , biology , mechanical engineering , engineering
The Front Cover shows the two kinds of interaction between Cu II and the amyloid‐β peptides involved in Alzheimer&s disease, depending on the sequences of the peptide (binding sites, affinity, and associated properties of the resulting Cu II –peptide species). While Cu II binding to the full‐length peptide is thought to be deleterious, especially by production of reactive oxygen species, Cu II binding to N‐terminally truncated forms seems to be harmless. The question “guilty or not guilty” will be answered in future… More information can be found in the Microreview by C. Hureau et al. For more on the story behind the cover research, see the Cover Profile .