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Frontispiece: Aggregation and Amyloidogenicity of the Nuclear Coactivator Binding Domain of CREB‐Binding Protein
Author(s) -
Garcia Ana Maria,
Giorgiutti Christophe,
El Khoury Youssef,
Bauer Valentin,
Spiegelhalter Coralie,
LeizeWagner Emmanuelle,
Hellwig Petra,
Potier Noelle,
Torbeev Vladimir
Publication year - 2020
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.202084471
Subject(s) - coactivator , enantiomer , creb , binding domain , chemistry , chirality (physics) , biophysics , plasma protein binding , domain (mathematical analysis) , binding site , stereochemistry , biochemistry , biology , physics , mathematics , transcription factor , mathematical analysis , nambu–jona lasinio model , chiral symmetry breaking , quantum mechanics , gene , quark
Aggregation and self‐assembly of nuclear coactivator binding domain of CREB‐binding protein was studied under different experimental conditions. Single l ‐ or d ‐enantiomers fold into left‐ or right‐handed helical structures at neutral pH while β‐sheet amyloid arrangement occurs under acidic conditions. Mixtures of both enantiomers promote self‐assembly into amyloid β‐sheet structures highlighting the role of chirality in the formation of thermodynamically more stable racemic β‐sheet structures. Fore more information, see the Full Paper by V. Torbeev et al. on page 9889 ff.