Frontispiece: Aggregation and Amyloidogenicity of the Nuclear Coactivator Binding Domain of CREB‐Binding Protein

Abstract

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.