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1.
Ultrason Sonochem ; 20(1): 610-7, 2013 Jan.
Article in English | MEDLINE | ID: mdl-22938998

ABSTRACT

Gold nanoparticles (NPs) are rapidly and efficiently formed under ambient conditions with a novel and highly-efficient sonochemical promoter. Despite of the presence of free oxygen, 3-glycidoxypropyltrimethoxysilane (GPTMS) showed remarkable efficiency in promoting the reduction rate of Au (III) than that of conventional promoters (primary alcohols). This is likely attributed to the formation of a variety of radical scavengers, which are alcoholic products from sonochemical hydrolysis of the epoxide group and methoxysilane moieties of GPTMS under weakly acidic conditions. Interestingly, the promotion is quenched by amine- or thiol-functionalized alkoxysilane, thereby producing marginal amounts of gold NPs. Furthermore, products of hydrolyzed GPTMS were confirmed to attach on the surface of gold NPs by attenuated total reflectance-Fourier transform infrared spectroscopy. However, according to transmission electron microscopy images, gold NPs that were produced in the presence of GPTMS tend to fuse with each other as condensation of silanols occurs, forming worm- or nugget-like gold nanostructures. The use of long chain surfactants (i.e. polyethylene glycol terminated with hydroxyl or carboxyl) inhibited the fusion, leading to mono-dispersed gold NPs. Additionally, the fact that this approach requires neither an ultrasound source with high frequency nor anaerobic conditions provides a huge advantage. These findings could potentially open an avenue for rapid and large-scale green-synthesis of gold NPs in future work.

2.
J Colloid Interface Sci ; 356(1): 182-9, 2011 Apr 01.
Article in English | MEDLINE | ID: mdl-21269638

ABSTRACT

Development of the nanodevice that myosin-coated beads "walk" on actin filaments (F-actin) tracks for in vitro nanotransportation was hindered due to the difficulty of assembling large-area well-orientated F-actin tracks on the surface. In this work, we present a selective attachment of F-actin with controlled length on a patterned surface by employing biotinylated capped protein gelsolin as intermediate anchoring bridge. A patterned streptavidin layer was formed via coupling with a biotin layer that photo-actively attached to an amine-functionalized glass surface. The patterned film was found stable and homogenous compared to that obtained by microcontact printing method, according to the profiling with fluorescence microscopy. By a secondary blocking process, non-specific binding of F-actin to the patterned surface through electrostatic adsorption can be resisted. The length variation of F-actin as a function of gelsolin concentration was also investigated, implying that F-actin is appropriately of 2.5 µm in average length once F-actin/gelsolin molar ratio is 4:1. Finally, the selective attachment of F-actin was well characterized with quantifying the number of attached F-actin per unit area in the patterned areas over that in blocked areas. The density of F-actin was estimated at c.a. 2 µm(2) per actin filament molecule so that the distance between one another actin filament is estimated as c.a. 1.41-1.97 µm. The unique properties of F-actin, e.g. well flexibility or electrical conductivity, make it feasible to lay them down and form unidirectional aligned tracks by fluidic flow or electrical field. This may open a possibility for the long-distant movement of myosin-coated beads, offering a novel discipline for the development of micro-biochip in vitro.


Subject(s)
Actin Cytoskeleton/metabolism , Actins/metabolism , Microfluidic Analytical Techniques/methods , Myosins/metabolism , Actin Cytoskeleton/chemistry , Actins/chemistry , Binding Sites , Biotin/chemistry , Biotin/metabolism , Biotinylation , Gelsolin/metabolism , Glass/chemistry , Microscopy, Fluorescence , Movement , Myosins/chemistry , Nanotechnology/methods , Protein Binding , Streptavidin/chemistry , Streptavidin/metabolism , Surface Properties
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