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Front Cover: Concentration‐Dependent Interactions of Amphiphilic PiB Derivative Metal Complexes with Amyloid Peptides Aβ and Amylin (Chem. Eur. J. 6/2021)
Author(s) -
Majdoub Saida,
Garda Zoltán,
Oliveira Alexandre C.,
Relich Inga,
Pallier Agnès,
Lacerda Sara,
Hureau Christelle,
Geraldes Carlos F. G. C.,
Morfin JeanFrançois,
Tóth Éva
Publication year - 2021
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.202004824
Subject(s) - amylin , amphiphile , amyloid (mycology) , chemistry , peptide , micelle , amyloid fibril , derivative (finance) , biophysics , aqueous solution , amyloid β , biochemistry , islet , insulin , disease , medicine , copolymer , biology , organic chemistry , inorganic chemistry , financial economics , economics , polymer
Metal chelates targeted to amyloid peptides are widely explored as diagnostic tools or therapeutic agents. Such amphiphilic chelates form pre‐micelles and micelles in aqueous solution. This work shows that the aggregation state strongly affects their affinity for Aβ 1‐40 or amylin amyloid fibrils, present in the brain and in the pancreas, and implicated in Alzheimer's disease or diabetes, respectively. More information can be found in the Full Paper by J.‐F. Morfin, É. Tóth et al. on page 2009.