Abstract
A better understanding of the compatibility of water-soluble semiconductor quantum dots (QDs) upon contact with the bloodstream is important for biological applications, including biomarkers working in the first therapeutic spectral window for deep tissue imaging. Herein, we investigated the conformational changes of blood plasma proteins during the interaction with near-infrared light-emitting nanoparticles, consisting of Pluronic F127 shells and cores comprised of assembled silicon QDs terminated with decane monolayers. Albumin and transferrin have high quenching constants and form a hard protein corona on the nanoparticle. In contrast, fibrinogen has low quenching constants and forms a soft protein corona. A circular dichroism (CD) spectrometric study investigates changes in the protein’s secondary and tertiary structures with incremental changes in the nanoparticle concentrations. As expected, the addition of nanoparticles causes the denaturation of the plasma proteins. However, it is noteworthy that the conformational recovery phenomena are observed for fibrinogen and transferrin, suggesting that the nanoparticle does not influence the ordered structure of proteins in the bloodstream. In addition, we observed enabled cellular uptake (NIH3T3 Fibroblasts) and minimal cytotoxicity using different cell lines (HeLa, A549, and NIH3T3). This study offers a basis to design QDs without altering the biomacromolecule’s original conformation with enabled cellular uptake with minimal cytotoxicity.
Highlights
Near-infrared (NIR) fluorescence light, which is broadly utilized for monitoring and imaging in minimally invasive medicine, provides researchers and surgeons highly specific images of target tissues in the living body [1,2,3,4,5]
PL and PL excitation (PLE) spectra of SiQD-De/F127 dispersed in Milli-Q water were measured using an InGaAs detector for NIR (Hamamatsu Photonics, Hamamatsu City, Japan) at room temperature on a NanoLog spectrofluorometer (Horiba Jovin Yvon, Tokyo, Japan) equipped with a 450 W xenon arc lamp
circular dichroism (CD) spectra of the plasma protein samples and the proteins complexed with SiQD-De/F127 were recorded with a spectropolarimeter (Jasco J-725, Tokyo, Japan) with 1 mm quartz cuvette at a scan speed of 100 nm/min at 25 ◦C
Summary
Near-infrared (NIR) fluorescence light, which is broadly utilized for monitoring and imaging in minimally invasive medicine, provides researchers and surgeons highly specific images of target tissues in the living body [1,2,3,4,5]. Blood contains high molecular weight proteins, such as albumin and globulin, which hamper the detection of low molecular weight proteins. Fibrinogen, and transferrin are essential proteins found in the blood. Albumin is the most abundant protein (55%) in the blood plasma. It involves transporting and delivering fatty acids, steroids, nutrients, and several therapeutic drugs. A detailed study on the plasma proteins interacting with NIR-SiQDs is lacking. We demonstrate the synthesis of water-borne NIR-SiQDs and their interactions with blood plasma proteins, albumin, fibrinogen, and transferrin. In addition to the above experiments, we demonstrated the nanomaterials’ cell viability test using three different types of cells (HeLa, A549 (cancer), and NIH3T3 (fibroblast)) and cellular uptake (NIH3T3) to check its compatibility
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