Angewandte Chemie International Edition
Copyright © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Cover Picture: Chemistry and Biology of the Aeruginosin Family of Serine Protease Inhibitors (Angew. Chem. Int. Ed. 7/2008)
Different phyla and different oceans are sources of linear peptides in the aeruginosin family which comprise a central hydroxy- (or dihydroxy-) octahydroindole carboxamide core unit onto which unusual amino acids are appended. The aeruginosins exhibit varying degrees of inhibitory activity against serine proteases, including factor II (thrombin) and factor VIIa of the blood coagulation cascade. In their Review on page 1202 ff., S. Hanessian et al. provide an overview of the chemical and biological properties of the aeruginosins as well as the natural sources of these compounds, their total syntheses, and structure revisions.
Also of Interest
Bodipy dyes, which were originally developed as luminescent tags and laser dyes, are well-suited for organic electronic materials and nanotechnology. In the Minireview on page 1184 ff., R. Ziessel and co-workers discuss this class of compounds.
Pulse EPR Spectroscopy
In their Communication on page 1224 ff., M. Bennati et al. describe the use of pulse EPR at high frequencies for the determination of both the distance between and the relative orientation of tyrosyl radicals within protein complexes.
In the Communication on page 1232 ff., F. Würthner and A. Lohr explain which factors are important for the homochirogenesis by self-assembly of bis(merocyanine) dyes.