The role of the medium in the effective-sphere interpretation of holographic particle characterization data

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Abstract

The in-line hologram of a micrometer-scale colloidal sphere can be analyzed with the Lorenz-Mie theory of light scattering to obtain precise measurements of the sphere’s diameter and refractive index. The same technique also can be used to characterize porous and irregularly shaped colloidal particles provided that the extracted parameters are interpreted with effective-medium theory to represent the properties of an equivalent effective sphere. Here, we demonstrate that the effective-sphere model consistently accounts for changes in the refractive index of the medium as it fills the pores of porous particles and therefore yields quantitative information about such particles’ structure and composition. In addition to the sample-averaged porosity, holographic perfusion porosimetry gauges the polydispersity of the porosity. We demonstrate these capabilities through measurements on mesoporous spheres, fractal protein aggregates and irregular nanoparticle agglomerates, all of which are noteworthy for their industrial significance.

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Synthesis of mesoporous silica nanoparticles.

Si-Han Wu, Chung-Yuan Mou, Hong-Ping Lin (2013)

Good control of the morphology, particle size, uniformity and dispersity of mesoporous silica nanoparticles (MSNs) is of increasing importance to their use in catalyst, adsorption, polymer filler, optical devices, bio-imaging, drug delivery, and biomedical applications. This review discusses different synthesis methodologies to prepare well-dispersed MSNs and hollow silica nanoparticles (HSNs) with tunable dimensions ranging from a few to hundreds of nanometers of different mesostructures. The methods include fast self-assembly, soft and hard templating, a modified Stöber method, dissolving-reconstruction and modified aerogel approaches. In practical applications, the MSNs prepared by these methods demonstrate good potential for use in high-performance catalysis, antireflection coating, transparent polymer-MSNs nanocomposites, drug-release and theranostic systems.

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Protein aggregation and its inhibition in biopharmaceutics.

Wei Wang (2005)

Protein aggregation is arguably the most common and troubling manifestation of protein instability, encountered in almost all stages of protein drug development. Protein aggregation, along with other physical and/or chemical instabilities of proteins, remains to be one of the major road barriers hindering rapid commercialization of potential protein drug candidates. Although a variety of methods have been used/designed to prevent/inhibit protein aggregation, the end results are often unsatisfactory for many proteins. The limited success is partly due to our lack of a clear understanding of the protein aggregation process. This article intends to discuss protein aggregation and its related mechanisms, methods characterizing protein aggregation, factors affecting protein aggregation, and possible venues in aggregation prevention/inhibition in various stages of protein drug development.