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Quantum Dots for Biomedical Applications

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Materials Science".

Deadline for manuscript submissions: 20 May 2025 | Viewed by 2959

Special Issue Editor


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Guest Editor
Institute for Integrated Cell-Material Sciences, Institute for Advanced Study, Kyoto University, Kyoto, Japan
Interests: biodegradable materials; mesoporous silica; silicon quantum dots; molecular interaction; cancer therapy

Special Issue Information

Dear Colleagues,

Quantum dots have recently gained more attention after being the focus of the 2023 Nobel Prize announcements. Quantum dots possess unique optical and electronic properties, such as fluorescence that can be controlled by their size, high quantum yields, and photobleaching stability. Due to these properties, they are well-suited for various applications, including optical labeling in multiplexed imaging, single-molecule probes, real-time imaging of tumors, in vivo deep tissue imaging, and drug delivery detection systems. Quantum dots that emit near-infrared light are particularly advantageous, as they can easily penetrate tissue. This makes them useful in guiding surgeons during tumor removal procedures.

We are excited to welcome a group of highly qualified contributors to this Special Issue. These contributors specialize in the application of quantum dots for molecular imaging, biosensing, medical diagnosis, drug delivery, and treatments.

Dr. Shanmugavel Chinnathambi
Guest Editor

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Keywords

  • quantum dots
  • molecular imaging
  • tissue imaging: biosensing
  • medical diagnosis
  • drug delivery

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Published Papers (2 papers)

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Research

13 pages, 2922 KiB  
Article
Analyzing Amylin Aggregation Inhibition Through Quantum Dot Fluorescence Imaging
by Xiaoyu Yin, Ziwei Liu, Gegentuya Huanood, Hayate Sawatari, Keiya Shimamori, Masahiro Kuragano and Kiyotaka Tokuraku
Int. J. Mol. Sci. 2024, 25(20), 11132; https://doi.org/10.3390/ijms252011132 - 17 Oct 2024
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Abstract
Protein aggregation is associated with various diseases caused by protein misfolding. Among them, amylin deposition is a prominent feature of type 2 diabetes. At present, the mechanism of amylin aggregation remains unclear, and this has hindered the treatment of type 2 diabetes. In [...] Read more.
Protein aggregation is associated with various diseases caused by protein misfolding. Among them, amylin deposition is a prominent feature of type 2 diabetes. At present, the mechanism of amylin aggregation remains unclear, and this has hindered the treatment of type 2 diabetes. In this study, we analyzed the aggregation process of amylin using the quantum dot (QD) imaging method. QD fluorescence imaging revealed that in the presence of 100 μM amylin, aggregates appeared after 12 h of incubation, while a large number of aggregates formed after 24 h of incubation, with a standard deviation (SD) value of 5.435. In contrast, 50 μM amylin did not induce the formation of aggregates after 12 h of incubation, although a large number of aggregates were observed after 24 h of incubation, with an SD value of 2.883. Confocal laser microscopy observations revealed that these aggregates were deposited in three dimensions. Transmission electron microscopy revealed that amylin existed as misfolded fibrils in vitro and that QDs were uniformly bound to the amylin fibrils. In addition, using a microliter-scale high-throughput screening (MSHTS) system, we found that rosmarinic acid, a polyphenol, inhibited amylin aggregation at a half-maximal effective concentration of 852.8 μM. These results demonstrate that the MSHTS system is a powerful tool for evaluating the inhibitory activity of amylin aggregation. Our findings will contribute to the understanding of the pathogenesis of amylin-related diseases and the discovery of compounds that may be useful in the treatment and prevention of these diseases. Full article
(This article belongs to the Special Issue Quantum Dots for Biomedical Applications)
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11 pages, 3451 KiB  
Article
Real-Time 3D Imaging and Inhibition Analysis of Human Serum Amyloid A Aggregations Using Quantum Dots
by Liangquan Shi, Gegentuya Huanood, Shuto Miura, Masahiro Kuragano and Kiyotaka Tokuraku
Int. J. Mol. Sci. 2024, 25(20), 11128; https://doi.org/10.3390/ijms252011128 - 16 Oct 2024
Viewed by 1070
Abstract
Serum amyloid A (SAA) is one of the most important precursor amyloid proteins discovered during the study of amyloidosis, but its underlying aggregation mechanism has not yet been well elucidated. Since SAA aggregation is a key step in the pathogenesis of AA amyloidosis, [...] Read more.
Serum amyloid A (SAA) is one of the most important precursor amyloid proteins discovered during the study of amyloidosis, but its underlying aggregation mechanism has not yet been well elucidated. Since SAA aggregation is a key step in the pathogenesis of AA amyloidosis, amyloid inhibitors can be used as a tool to study its pathogenesis. Previously, we reported a novel microliter-scale high-throughput screening (MSHTS) system for screening amyloid β (Aβ) aggregation inhibitors based on quantum dot (QD) fluorescence imaging technology. In this study, we report the aggregation of human SAA (hSAA) in phosphate-buffered saline, in which we successfully visualized hSAA aggregation by QD using fluorescence microscopy and confocal microscopy. Two-dimensional and three-dimensional image analyses showed that most aggregations were observed at 40 μM hSAA, which was the optimal aggregation concentration in vitro. The accuracy of this finding was verified by a Thioflavin T assay. The transmission electron microscopy results showed that QD uniformly bound to hSAA aggregation. hSAA aggregation inhibitory activity was also evaluated by rosmarinic acid (RA). The results showed that RA, which is a compound with high inhibitory activity against Aβ aggregation, also exhibited high inhibitory activity against 40 μM hSAA. These results indicate that the MSHTS system is an effective tool for visualizing hSAA aggregation and for screening highly active inhibitors. Full article
(This article belongs to the Special Issue Quantum Dots for Biomedical Applications)
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