Strategies for the selective loading of patchy worm-like micelles with functional nanoparticles.

Block copolymer self-assembly in solution paves the way for the construction of well-defined compartmentalized nanostructures. These are excellent templates for the incorporation and stabilisation of nanoparticles (NPs), giving rise to highly relevant applications in the field of catalysis or sensing. However, the regio-selective incorporation of NPs in specific compartments is still an issue, especially concerning the loading with different NP types.

Template Removal via Boudouard Equilibrium Allows for Synthesis of Mesostructured Molybdenum Compounds.

Oxidative thermal removal of the polymeric templates is not trivial for molybdenum oxides and hampers mesostructuring of this material. At ambient oxygen fugacity, Mo is the thermodynamically stable oxidation state and sublimation of MoO leads to a quick loss of the mesostructure through Oswald ripening. Taking advantage of the Boudouard equilibrium allows to fix the oxygen fugacity at a level where non-volatile MoO is stable while carbonaceous material may be oxidized by CO .

Direct synthesis of inverse hexagonally ordered diblock copolymer/polyoxometalate nanocomposite films.

Nanostructured inverse hexagonal polyoxometalate composite films were cast directly from solution using poly(butadiene-block-2-(dimethylamino)ethyl methacrylate) (PB-b-PDMAEMA) diblock copolymers as structure directing agents for phosphomolybdic acid (H(3)[PMo(12)O(40)], H(3)PMo). H(3)PMo units are selectively incorporated into the PDMAEMA domains due to electrostatic interactions between protonated PDMAEMA and PMo(3-) anions. Long solvophilic PB chains stabilized the PDMAEMA/H(3)PMo aggregates in solution and reliably prevented macrophase separation.

Molecular cloning and expression of an avian rab5 homolog.

A chicken rab5 cDNA was isolated that contains the complete open reading frame for a protein of 216 amino acids, which, by comparison with available rab5 sequences from other species, is most closely related to the rab5c isoform. Two rab5 transcripts of 1.3 and 1.