Angewandte Chemie International Edition

Cover image for Vol. 54 Issue 11

Editor: Peter Gölitz, Deputy Editors: Neville Compton, Haymo Ross

Online ISSN: 1521-3773

Associated Title(s): Angewandte Chemie, Chemistry - A European Journal, Chemistry – An Asian Journal, ChemistryOpen, ChemPlusChem, Zeitschrift für Chemie

54_10/2015Cover Picture: The Catalytic Mechanism of Human Parainfluenza Virus Type 3 Haemagglutinin-Neuraminidase Revealed (Angew. Chem. Int. Ed. 10/2015)

The human parainfluenza virus type 3 (hPIV-3) is one of the leading causes of lower respiratory tract disease in children. In their Communication on page 2936 ff., M. von Itzstein, I. M. El-Deeb, P. Guillon, L. M. G. Chavas, and co-workers investigate the catalytic mechanism of hPIV-3 haemagglutinin-neuraminidase (HN) and determine that it is a retaining glycohydrolase. Moreover hPIV-3 HN utilizes a highly conserved tyrosine residue to form a transient covalent bond with the anomeric carbon of the substrate. Finally a novel sialic acid derivative showed potency in virus blockade assays.

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Also of Interest

The human parainfluenza virus type 3 (hPIV-3) is one of the leading causes of lower respiratory tract disease in children. In their Communication on page 2936 ff., M. von Itzstein, I. M. El-Deeb, P. Guillon, L. M. G. Chavas, and co-workers investigate the catalytic mechanism of hPIV-3 haemagglutinin-neuraminidase (HN) and determine that it is a retaining glycohydrolase. Moreover hPIV-3 HN utilizes a highly conserved tyrosine residue to form a transient covalent bond with the anomeric carbon of the substrate. Finally a novel sialic acid derivative showed potency in virus blockade assays.

Nanoparticlesfor001

K. M. Fromm, B. Giese et al. report in their Communication on page 2912 ff. how shielding effects prevent the formation of Ag nanoparticles from Ag+–peptides. This problem was overcome by chloride ions first forming AgCl microcrystals.


Microwave Spectroscopyfor002

In their Communication on page 2991 ff., J. L. Alonso et al. show that intramolecular hydrogen bonds involving uracil and ribose moieties play an important role in the stabilization of the nucleoside uridine.


Blood–Brain Barrierfor003

In their Communication on page 3023 ff., W. Lu, C. Zhan, et al. identified a d-peptide ligand of nicotine acetylcholine receptors that is resistant to proteolysis and verified its superiority for brain-targeted drug delivery over the l-peptide ligand.


54_10i/2015Inside Cover: A Complex Perovskite-Type Oxynitride: The First Photocatalyst for Water Splitting Operable at up to 600 nm (Angew. Chem. Int. Ed. 10/2015)

Water splitting on a particulate-type photocatalyst using solar energy is expected to be a scalable and cost-effective route for hydrogen production. However, most of the photocatalysts developed to date can only utilize a small part of the spectrum of sunlight. In their Communication on page 2955 ff., T. Takata, K. Domen et al. describe the development of a novel water-splitting photocatalyst operable over a wide range of the visible-light spectrum.

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54_10c/2015Inside Back Cover: The Nucleoside Uridine Isolated in the Gas Phase (Angew. Chem. Int. Ed. 10/2015)

The nucleoside uridine has been placed in the gas phase by laser ablation and structurally characterized by Fourier transform microwave spectroscopy. In their Communication on page 2991 ff., J. L. Alonso et al. show that free from the bulk effects of their native environments, the anti/C2'-endo-g+ conformation is the most stable form. Intramolecular hydrogen bonds involving uracil and ribose moieties play an important role in the stabilization of the nucleoside.

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54_10b/2015Back Cover: A d-Peptide Ligand of Nicotine Acetylcholine Receptors for Brain-Targeted Drug Delivery (Angew. Chem. Int. Ed. 10/2015)

Peptide ligands efficiently aid brain-targeted drug delivery by hijacking cognate receptors expressed on brain capillary endothelial cells. However, enzymatic barriers inactivate l-peptides and undermine the transport efficiency. In their Communication on page 3023 ff., W. Lu, C. Zhan, et al. identified a d-peptide ligand of nicotine acetylcholine receptors that is resistant to proteolysis and verified its superiority for brain-targeted drug delivery in comparison to the l-peptide ligand.

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