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.
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