Layer-by-layer assembled titania tubular nanostructures at different assembly conditions.

Layer-by-layer (LbL) deposition of poly(L-lysine) (PLL) dissolved in different solutions and a water-soluble titania precursor, titanium(IV) bis(ammonium lactate) dihydroxide (TiBALDH) to form multilayer films on the wall of polycarbonate (PC) membrane pores was performed to prepare nanostructured titania-PLL composite and pure anatase and rutile titania tubes. A battery of analytical techniques was utilized to characterize and compare the structures, crystal phases, and photocatalytic properties of the titania tubes. In different solutions conditions, PLL which adopts secondary conformations (i.e., alpha-helix and random coil) and has varying interactions with different counterions (i.e., chloride and phosphate ions) can influence PLL/TiBALDH deposition and, in turn, results in the titania materials with different nanostructures and phtocatalytic properties. The influence of LbL assembly condition, deposition cycle, and polypeptide molecular weight on photocatalytic properties of resultant anatase titania tubes were further explored and these materials are promising photocatalyst with the advantage of easily handling and recycling. This reported approach may provide a facile and general way to prepare organic-inorganic composite and other inorganic materials with different compositions, structures, and properties for various applications.

Layer-by-layer polypeptide macromolecular assemblies-mediated synthesis of mesoporous silica and gold nanoparticle/mesoporous silica tubular nanostructures.

A simple and versatile approach is proposed to use the LbL-assembled polypeptide macromolecular assemblies as mediating agents and templates for directed growth of gold nanoparticles and biomimetic silica mineralization, allowing the synthesis of polypeptide/silica and polypeptide/gold nanoparticle/silica composite materials, as well as mesoporous silica (meso-SiO2) and gold nanoparticle/mesoporous silica (Au NP/meso-SiO2). The formation of tubular nanostructures was demonstrated by silicification and growth of gold nanoparticles within macromolecular assemblies formed by poly(L-lysine) (PLL) and poly(L-glutamic acid) (PLGA) using polycarbonate membranes as templates. The experimental data revealed that the silicified macromolecular assemblies adopted mainly sheet/turn conformation. The as-prepared mesoporous silica materials possessed well-defined tubular structures with pore size and porosity depending on the size of sheet/turn aggregates, which is a function of the molecular weight of polypeptides. The directed growth of Au NP and subsequent silica mineralization in the macromolecular assembly resulted in Au NP/meso-SiO2 tubes with uniform nanoparticle size and the as-prepared materials exhibited promising catalytic activity toward the reduction of p-nitrophenol. This approach provides a facile and general method to synthesize organic-inorganic composite materials, oxide and metal-oxide nanomaterials with different compositions and structures.

Efficient and stable enzyme immobilization in a block copolypeptide vesicle-templated biomimetic silica support.

We report the immobilization of a model enzyme, papain, within silica matrices by combining vesiclization of poly-l-lysine-b-polyglycine block copolypeptides with following silica mineralization. Our novel strategy utilizes block polypeptide vesicles to induce the condensation of orthosilicic acid while trapping an enzyme within and between vesicles. The polypeptide mediated silica-immobilized enzyme exhibits enhanced pH and thermal stability and reusability, comparing with the free and vesicle encapsulated enzyme. The enhanced enzymatic activity in the immobilized enzyme is due to the confinement of the enzyme in the polypeptide mediated silica matrices. Kinetic analysis shows that the enzyme functionality is determined by the structure and property of silica/polypeptide matrices. The proposed novel strategy provides an alternative route for the synthesis of a broad range of functional bionanocomposites entrapped within silica nanostructures.

The proximity between C-termini of dimeric vacuolar H+-pyrophosphatase determined using atomic force microscopy and a gold nanoparticle technique.

Vacuolar H(+)-translocating inorganic pyrophosphatase [vacuolar H(+)-pyrophosphatase (V-PPase); EC 3.6.1.1] is a homodimeric proton translocase; it plays a pivotal role in electrogenic translocation of protons from the cytosol to the vacuolar lumen, at the expense of PP(i) hydrolysis, for the storage of ions, sugars, and other metabolites. Dimerization of V-PPase is necessary for full proton translocation function, although the structural details of V-PPase within the vacuolar membrane remain uncertain. The C-terminus presumably plays a crucial role in sustaining enzymatic and proton-translocating reactions. We used atomic force microscopy to visualize V-PPases embedded in an artificial lipid bilayer under physiological conditions. V-PPases were randomly distributed in reconstituted lipid bilayers; approximately 43.3% of the V-PPase protrusions faced the cytosol, and 56.7% faced the vacuolar lumen. The mean height and width of the cytosolic V-PPase protrusions were 2.8 +/- 0.3 nm and 26.3 +/- 4.7 nm, whereas those of the luminal protrusions were 1.2 +/- 0.1 nm and 21.7 +/- 3.6 nm, respectively. Moreover, both C-termini of dimeric subunits of V-PPase are on the same side of the membrane, and they are close to each other, as visualized with antibody and gold nanoparticles against 6xHis tags on C-terminal ends of the enzyme. The distance between the V-PPase C-terminal ends was determined to be approximately 2.2 +/- 1.4 nm. Thus, our study is the first to provide structural details of a membrane-bound V-PPase dimer, revealing its adjacent C-termini.