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Analysis of Silicon Quantum Dots and Serum Proteins Interactions Using Asymmetrical Flow Field-Flow Fractionation
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DOI：10.1021/acs.langmuir.3c00109.png)
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Abstract
En 中文
Semiconductor nanocrystals or quantum dots (QDs) havegained significantattention in biomedical research as versatile probes for imaging,sensing, and therapies. However, the interactions between proteinsand QDs, which are crucial for their use in biological applications,are not yet fully understood. Asymmetric flow field-flow fractionation(AF4) is a promising method for analyzing the interactions of proteinswith QDs. This technique uses a combination of hydrodynamic and centrifugalforces to separate and fractionate particles based on their size andshape. By coupling AF4 with other techniques, such as fluorescencespectroscopy and multi-angle light scattering, it is possible to determinethe binding affinity and stoichiometry of protein-QD interactions.Herein, this approach has been utilized to determine the interactionbetween fetal bovine serum (FBS) and silicon quantum dots (SiQDs).Unlike metal-containing conventional QDs, SiQDs are highly biocompatibleand photostable in nature, making them attractive for a wide rangeof biomedical applications. In this study, AF4 has provided crucialinformation on the size and shape of the FBS/SiQD complexes, theirelution profile, and their interaction with serum components in realtime. The differential scanning microcalorimetric technique has alsobeen employed to monitor the thermodynamic behavior of proteins inthe presence of SiQDs. We have investigated their binding mechanismsby incubating them at temperatures below and above the protein denaturation.This study yields various significant characteristics such as theirhydrodynamic radius, size distribution, and conformational behavior.The compositions of SiQD and FBS influence the size distribution oftheir bioconjugates; the size increases by intensifying the concentrationof FBS, with their hydrodynamic radii ranging between 150 and 300nm. The results signify that in the alliance of SiQDs to the system,there is an augmentation of the denaturation point of the proteinsand hence their thermal stability, providing a more comprehensiveunderstanding of the interactions between FBS and QDs.
Keywords:
CARBON DOTS
NANOPARTICLES
AGGREGATION
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