Cover Picture: Seed-mediated Growth of Gold inside Hollow Silica Nanospheres for Sensing Peroxide and Glucose Concentrations (Chem. Asian J. 1/2012)

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Abstract

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A common limitation of gold nanoparticle (Au NP)-based sensing in natural samples is that non-specific binding of biomolecules on the Au NP surface interferes in sensing systems and causes a reduction in the selectivity and sensitivity. To circumvent such a limitation, a recently developed hollow nanoreactor with a nanorattle structure, consisting of a porous silica nanoshell and an entrapped Au NP, was employed. As described in their Communication on page 36 ff., I. S. Lee et al. report that the catalytic Au growth inside the protected cavity, which is accompanied by an SPR enhancement, allows for the quantitative detection of H2O2 and glucose concentrations, even in the presence of the interfering BSA proteins.

Total synthesis

Englerin A is a recently reported guaiane sesquiterpenoid characterized by its densely functionalized 5-6-5 oxo-bridged tricyclic system with seven stereogenic centers embedded. In conjunction with its potent and selective anti-cancer property, englerin A received immediate attention from the synthetic community as an fertile testing ground for modern synthetic technologies and strategies. In their Focus Review on page 22 ff., D. Y.-K. Chen et al. discuss the contrasting approaches developed for the synthesis of englerin A originating from the laboratories of the pictured researchers, showcasing the state-of-the-art synthetic organic chemistry and setting the stage for the development of novel chemotherapeutics.

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Chemoenzymatic synthesis

In their Full Paper on page 64 ff., S. Aoki et al. demonstrate that all possible stereoisomers of 1,3-diols can be produced with high diastereo- and enantioselectivities by a one-pot chemoenzymatic synthesis in water. The synthesis involves an enantioselective aldol reaction catalyzed by a chiral Zn2+-complex catalyst and successive enantioselective reduction of the aldol product using an oxidoreductase, with regeneration of NADH.

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