Angewandte Chemie International Edition
© WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Cover Picture: Dissociation of Amyloid Fibrils of α-Synuclein in Supercooled Water (Angew. Chem. Int. Ed. 27/2008)
Amyloid fibrils are filamentous aggregates of peptides and proteins with exceptional stability that are associated with several neurodegenerative diseases. M. Zweckstetter et al. demonstrate in their Communication on page 5046 ff. that amyloid fibrils formed by the protein α-synuclein, which is associated with Parkinson's disease, are rapidly denatured, that is, dissociated and lose the conformation of the constituent protein molecules, in supercooled water at −15 °C, conditions in which many globular proteins remain folded.
Also of Interest
Gas Storage Materials
The current state-of-the-art in terms of gas storage in nanoporous materials is summarized in the Review by R. E. Morris and P. S. Wheatley on page 4966 ff. The most important fields are gas storage for energy, environmental, and medical applications.
In their Communication on page 4982 ff., R. Kniep, D. Zahn et al. show how ion association in apatite–collagen composites promotes peculiar motifs in the apatite crystal structure.
A. Fürstner and L. Morency show in their Communication on page 5030 ff. that the intermediates in gold-catalyzed cycloisomerizations are, in accord with the Stork–Eschenmoser postulate, more adequately described as gold-stabilized carbocations than as gold carbenes.