The inline coupling of the field-amplified sample injection (FASI) to Taylor dispersion analysis (TDA) was used to characterize low-UV absorbing carboxylated silica nanoparticles (cNPs). The hydrodynamic diameters (D) were measured by using a commercial capillary electrophoresis instrument. The proposed methodology did not require any complicated instruments or chromophoric dye to increase the detection sensitivity. A practical method based on a half-Gaussian fitting was proposed for the data processing. The results obtained by this method were compared with those derived from dynamic light scattering (DLS) and transmission electron microscopy (TEM) analyses. From these results, it appeared that the size derived by TDA is in excellent agreement with those measured by DLS and TEM, as demonstrated by stable nanoparticles with narrow size distributions. Intermediate precision relative standard deviations less than 5% were obtained by FASI-TDA. The effect of the FASI-induced cNP peak dispersion on the reliability of the results was discussed in detail.
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http://dx.doi.org/10.1021/acs.analchem.7b03344 | DOI Listing |
J Colloid Interface Sci
January 2025
Department of Chemical Engineering, National Tsing Hua University, No. 101, Sec. 2, Kuang-Fu Rd. 300044 Hsinchu City, Taiwan, ROC. Electronic address:
This study presents a novel approach for the controlled synthesis and real-time characterization of crosslinked hyaluronic acid (HA) hydrogels utilizing a microfluidic platform coupled with hyphenated electrospray-differential mobility analysis (ES-DMA). By precisely controlling key synthesis parameters within the microfluidic environment, including pH, temperature, reaction time, and the molar ratio of HA to crosslinker (1,4-butanediol diglycidyl ether, BDDE), we successfully synthesized HA hydrogels with tailored size and properties. The integrated ES-DMA system provides rapid, in-line analysis of hydrogel particle size and distribution, enabling real-time monitoring and optimization of the synthesis process.
View Article and Find Full Text PDFAnal Chem
January 2025
Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana 46556, United States.
Intact protein analysis using mass spectrometry (MS) is an important technique to characterize and provide a comprehensive overview of protein complexity. It is also the basis of "top-down" approaches in proteomics to describe the proteoforms of single protein's post-translational modifications (PTMs). MS-based analysis of intact proteins benefits from high-resolution separations prior to electrospray ionization.
View Article and Find Full Text PDFActa Crystallogr F Struct Biol Commun
January 2025
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF), UMR 8576 CNRS and University of Lille, Villeneuve d'Ascq, France.
Monoclonal antibodies recognizing nonprotein antigens remain largely underrepresented in our understanding of the molecular repertoire of innate and adaptive immunity. One such antibody is Mannitou, a murine IgM that recognizes paucimannosidic glycans. In this work, we report the production and purification of the recombinant antigen-binding fragment (Fab) of Mannitou IgM (Mannitou Fab) and employ a combination of biochemical and biophysical approaches to obtain its initial structural characterization.
View Article and Find Full Text PDFElife
December 2024
Department of Aerospace and Mechanical Engineering, University of Southern California, Los Angeles, United States.
The coordinated motion of animal groups through fluids is thought to reduce the cost of locomotion to individuals in the group. However, the connection between the spatial patterns observed in collectively moving animals and the energetic benefits at each position within the group remains unclear. To address this knowledge gap, we study the spontaneous emergence of cohesive formations in groups of fish, modeled as flapping foils, all heading in the same direction.
View Article and Find Full Text PDFNanophotonics
March 2024
State Key Laboratory of Information Photonics and Optical Communications, Beijing University of Posts and Telecommunications, Beijing 100876, China.
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