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1.
Faraday Discuss ; 191: 73-88, 2016 10 06.
Article in English | MEDLINE | ID: mdl-27442153

ABSTRACT

We present a new class of organic-inorganic patchy particles for the efficient stabilization of Pickering foams and emulsions. Using solvent-based heterogeneous precipitation, we decorate inorganic silica particles with discrete domains of water insoluble plant protein (zein). By varying the extent of protein coverage on the silica surface, we tune the pH-dependent interactions of the particles and the interfaces. We observe an optimum foam stabilization, which is attributed to the creation of a slightly positive low effective surface potential from positively charged protein patches and the negatively charged silica surface. The effect of surface coverage on foam stability is in line with the predicted low interfacial potential of the patchy particles in water, which determines the energy of particle adsorption. In emulsions, the increase of the protein amount on the silica particles causes a progressive bridging of the oil droplets into a close-packing configuration due to gelation of the protein patches. Protein-based organic-inorganic surface heterogeneous particles represent a new versatile platform for the stabilization of fluid-in-fluid dispersions and as precursors for the assembly of advanced functional materials.

2.
Ultrasound Med Biol ; 30(3): 397-404, 2004 Mar.
Article in English | MEDLINE | ID: mdl-15063522

ABSTRACT

The effectiveness of magnetic resonance imaging (MRI) to monitor therapeutic protocols of high-intensity focused ultrasound (HIFU), in freshly excised pig kidney cortex is investigated. For high quality imaging, the pulse sequence fast spin echo (FSE) T1- and T2-weighted, and proton density were evaluated. For fast imaging, the pulse sequence T1-weighted fast spoiled gradient (FSPGR) was used. The main goal was to evaluate the MRI detection of large lesions (bigger than 1 cm x 1 cm x 1 cm) that is achieved by moving the transducer in a predetermined pattern. The contrast between lesion and kidney tissue is excellent with either T1-weighted or T2-weighted FSE. With T1-weighted FSE, the best contrast is observed for recovery time (TR) between 200 ms and 400 ms. With T2-weighted FSE best contrast can be achieved for echo time (TE) between 16 and 32 ms. T2-weighted FSE was proven as the best pulse sequence to detect cavitational activity. This advantage is attributed to the significant difference in signal intensity between air spaces and necrotic tissue. Air spaces appear brighter than thermal lesions. Therefore, for therapeutic protocols created using cavitational mode, T2-weighted FSE may be the optimum pulse sequence to use. The proton density pulse sequence does not provide any advantage over the T1- and T2-weighted pulse sequences. Using T1-weighted FSPGR, acquisition time as low as 5 s could be achieved. Good contrast and signal-to-noise ratio (SNR) are achieved with TR = 100 ms and flip angle between 75 to 90 degrees. The above techniques were very successful in detecting large lesion volumes.


Subject(s)
Kidney/pathology , Magnetic Resonance Imaging/methods , Ultrasonic Therapy/methods , Animals , Magnetic Resonance Imaging/instrumentation , Necrosis , Swine , Transducers
3.
Science ; 294(5544): 1082-6, 2001 Nov 02.
Article in English | MEDLINE | ID: mdl-11691987

ABSTRACT

A new class of microwires can be assembled by dielectrophoresis from suspensions of metallic nanoparticles. The wires are formed in the gaps between planar electrodes and can grow faster than 50 micrometers per second to lengths exceeding 5 millimeters. They have good ohmic conductance and automatically form electrical connections to conductive islands or particles. The thickness and the fractal dimension of the wires can be controlled, and composite wires with a metallic core surrounded by a latex shell can be assembled. The simple assembly process and their high surface-to-volume ratio make these structures promising for wet electronic and bioelectronic circuits.

4.
Biophys J ; 75(6): 2682-97, 1998 Dec.
Article in English | MEDLINE | ID: mdl-9826592

ABSTRACT

The effects of pH and electrolyte concentration on protein-protein interactions in lysozyme and chymotrypsinogen solutions were investigated by static light scattering (SLS) and small-angle neutron scattering (SANS). Very good agreement between the values of the virial coefficients measured by SLS and SANS was obtained without use of adjustable parameters. At low electrolyte concentration, the virial coefficients depend strongly on pH and change from positive to negative as the pH increases. All coefficients at high salt concentration are slightly negative and depend weakly on pH. For lysozyme, the coefficients always decrease with increasing electrolyte concentration. However, for chymotrypsinogen there is a cross-over point around pH 5.2, above which the virial coefficients decrease with increasing ionic strength, indicating the presence of attractive electrostatic interactions. The data are in agreement with Derjaguin-Landau-Verwey-Overbeek (DLVO)-type modeling, accounting for the repulsive and attractive electrostatic, van der Waals, and excluded volume interactions of equivalent colloid spheres. This model, however, is unable to resolve the complex short-ranged orientational interactions. The results of protein precipitation and crystallization experiments are in qualitative correlation with the patterns of the virial coefficients and demonstrate that interaction mapping could help outline new crystallization regions.


Subject(s)
Proteins/chemistry , Animals , Biophysical Phenomena , Biophysics , Cattle , Chemical Precipitation , Chickens , Chymotrypsinogen/chemistry , Crystallization , Electrolytes , Hydrogen-Ion Concentration , Light , Macromolecular Substances , Muramidase/chemistry , Neutrons , Scattering, Radiation , Solutions , Static Electricity
5.
Adv Biophys ; 34: 139-57, 1997.
Article in English | MEDLINE | ID: mdl-9204132

ABSTRACT

We investigate different schemes for fabrication of nanometer sized assemblies that consist of a liposome core over which a shell of ferritin is attached. Three distinct interactions were used for this assembly: (i) Electrostatic attraction. The liposomes are charged by the presence of cationic surfactant (HTAB) and at an appropriate pH collect the ferritin molecules into a 2D-ordered ferritin shell. The protein shells can be fixed by glutaraldehyde. Next, the liposomes can be removed by solubilisation, leaving behind ordered ferritin clusters. (ii) Specific avidin-biotin or streptavidin-biotin binding. The ferritin molecules are conjugated to avidin or streptavidin and the liposomes incorporate biotinylated lipid. We found that the specific binding can be completely blocked by unfavourable electrostatic repulsion. To adjust the appropriate liposome charge we include cationic surfactant in the lipid layer. Thus, to accomplish the assembly process, we need to design and modify both the specific and non-specific colloid interactions in the system. The result is liposomes heavily coated with a strongly and specifically attached ferritin layer. (iii) Specific polysaccharide/lectin binding. The liposomes are first coated with a cholesterol-anchored mannan layer. The ferritin molecules are conjugated with Con A that binds to the polysaccharide. A smooth and dense coating with ferritin is obtained (Fig. 3b). The acquired data can find application in the future fabrication of microstructured, multicomponent, or functionalised protein and liposome/ protein assemblies.


Subject(s)
Ferritins/chemistry , Ferritins/ultrastructure , Liposomes/chemistry , Proteins/chemistry , Proteins/ultrastructure , Avidin/chemistry , Bacterial Proteins/chemistry , Biotin/chemistry , Cross-Linking Reagents , Glutaral , Microscopy, Electron , Phosphatidylcholines , Static Electricity , Streptavidin , Surface-Active Agents
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