Publications by authors named "Carmen R M Bria"

Field-flow fractionation (FFF) is a family of techniques that was created especially for separating and characterizing macromolecules, nanoparticles, and micrometer-sized analytes. It is coming of age as new nanomaterials, polymers, composites, and biohybrids with remarkable properties are introduced and new analytical challenges arise due to synthesis heterogeneities and the motivation to correlate analyte properties with observed performance. Appreciation of the complexity of biological, pharmaceutical, and food systems and the need to monitor multiple components across many size scales have also contributed to FFF's growth.

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High- and low-density lipoproteins (HDL and LDL) are attractive targets for biomarker discovery. However, ultracentrifugation (UC), the current methodology of choice for isolating HDL and LDL, is tedious, requires large sample volume, results in sample loss, and does not readily provide information on particle size. In this work, human plasma HDL and LDL are separated and collected using semi-preparative asymmetrical flow field-flow fractionation (SP-AF4) and UC.

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The design and performance of a semi-preparative asymmetrical flow field-flow fractionation (SP-AF4) channel are investigated with the objective of better understanding and exploiting the relationship between channel dimensions, sample loading, and resolution. Most size-based separations of nanometer and submicrometer particles are currently limited to analytical scale quantities (<100μg). However, there is a strong need to fractionate and collect larger quantities so that fundamental properties of the more narrowly dispersed fractions can be studied using additional characterization methods and for subsequent applications.

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Polymer self-assemblies joining oppositely charged chains, known as polyion complexes (PICs), have been formed using poly(ethyleneoxide - b - acrylic acid)/poly(l-lysine), poly(ethyleneoxide-b-acrylic acid)/dendrigraft poly(l-lysine) and poly[(3-acrylamidopropyl) trimethylammonium chloride - b - N - isopropyl acrylamide]/poly(acrylic acid). The self-assemblies have been first characterized in batch by Dynamic Light Scattering. In a second step, their analysis by Flow Field-Flow Fractionation techniques (FlFFF) was examined.

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The impact of asymmetrical flow field-flow fractionation (AF4) on protein aggregate species is investigated with the aid of multiangle light scattering (MALS) and dynamic light scattering (DLS). The experimental parameters probed in this study include aggregate stability in different carrier liquids, shear stress (related to sample injection), sample concentration (during AF4 focusing), and sample dilution (during separation). Two anti-streptavidin (anti-SA) IgG1 samples composed of low and high molar mass (M) aggregates are subjected to different AF4 conditions.

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A lack of reliable analytical methods has hindered the quantification of submicron protein aggregates and a detailed understanding of their formation kinetics. In this study, a simple asymmetrical flow field-flow fractionation (AF4) method with good size selectivity (>0.5) is used to investigate nanometer (<0.

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This paper reports the first use of a remote sensing device to measure emissions from in-use marine vessels. Emissions from 307 small marine vessels were measured as they passed through the Hiram M. Chittenden locks near Seattle, WA.

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