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Molecular interaction of silicon quantum dot micelles with plasma proteins: hemoglobin and thrombin
- Chinnathambi, Shanmugavel, Karthikeyan, Subramani, Hanagata, Nobutaka, Shirahata, Naoto
- RSC advances 2019 v.9 no.26 pp. 14928-14936
- binding capacity, circular dichroism spectroscopy, computer simulation, cytotoxicity, drug carriers, fluorescence emission spectroscopy, hemoglobin, micelles, molecular dynamics, nanoparticles, protein folding, quantum dots, silicon, simulation models, thrombin, water solubility
- Protein conformational changes are associated with potential cytotoxicity upon interaction with small molecules or nanomaterials. Protein misfolding leads to protein-mediated diseases; thus, it is important to study the conformational changes in proteins using nanoparticles as drug carriers. In this study, the conformational changes in hemoglobin and thrombin were observed using fluorescence spectroscopy, circular dichroism spectroscopy and molecular modelling studies after interaction with non-toxic, water-soluble near-infrared silicon quantum dot micelles. The molecular docking results indicated that the binding affinities of hemoglobin and thrombin with Si QD micelles are good. In addition, molecular dynamics simulations were performed to obtain more detailed information.