1. Structural changes in selected human proteins induced by exposure to quantum dots, their biological relevance and possible biomedical applications.
- Author
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Kunachowicz D, Ściskalska M, Jakubek M, Kizek R, and Kepinska M
- Subjects
- Humans, Luminescence, Nanoparticles chemistry, Quantum Dots chemistry
- Abstract
Quantum dots (QDs) are semi-conductor luminescent nanocrystals usually of 2-10 nm diameter, attracting the significant attention in biomedical studies since emerged. Due to their unique optical and electronic properties, i.e. wide absorption spectra, narrow tunable emission bands or stable, bright photoluminescence, QDs seem to be ideally suited for multi-colour, simultaneous bioimaging and cellular labeling at the molecular level as new-generation probes. A highly reactive surface of QDs allows for conjugating them to biomolecules, what enables their direct binding to areas of interest inside or outside the cell for biosensing or targeted delivery. Particularly protein-QDs conjugates are current subjects of research, as features of QDs can be combined with protein specific functionalities and therefore used as a complex in variety of biomedical applications. It is known that QDs are able to interact with cells, organelles and macromolecules of the human body after administration. QDs are reported to cause changes at proteins level, including unfolding and three-dimensional structure alterations which might hamper proteins from performing their physiological functions and thereby limit the use of QD-protein conjugates in vivo. Moreover, these changes may trigger unwanted cellular outcomes as the effect of different signaling pathways activation. In this review, characteristics of QDs interactions with certain human proteins are presented and discussed. Besides that, the following manuscript provides an overview on structural changes of specific proteins exposed to QDs and their biological and biomedical relevance., (Copyright © 2022 The Authors. Published by Elsevier B.V. All rights reserved.)
- Published
- 2022
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