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Eco-friendly synthesis of CuInS(2) and CuInS(2)@ZnS quantum dots and their effect on enzyme activity of lysozyme
We report on the green and facile aqueous microwave synthesis of glutathione (GSH) stabilized luminescent CuInS(2) (CIS, size = 2.9 nm) and CuInS(2)@ZnS core–shell (CIS@ZnS, size = 3.5 nm) quantum dots (QDs). The core–shell nanostructures exhibited excellent photo- and water/buffer stability, a long...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9085571/ https://www.ncbi.nlm.nih.gov/pubmed/35546847 http://dx.doi.org/10.1039/c8ra04866e |
Sumario: | We report on the green and facile aqueous microwave synthesis of glutathione (GSH) stabilized luminescent CuInS(2) (CIS, size = 2.9 nm) and CuInS(2)@ZnS core–shell (CIS@ZnS, size = 3.5 nm) quantum dots (QDs). The core–shell nanostructures exhibited excellent photo- and water/buffer stability, a long photoluminescence (PL) lifetime (463 ns) and high PL quantum yield (PLQY = 26%). We have evaluated the comparative enzyme kinetics of these hydrophilic QDs by interacting them with the model enzyme lysozyme, which was probed by static and synchronous fluorescence spectroscopy. The quantification of the QD–lysozyme binding isotherm, exchange rate, and critical flocculation concentration was carried out. The core–shell QDs exhibited higher binding with lysozyme yielding a binding constant of K = 5.04 × 10(9) L mol(−1) compared to the core-only structures (K = 6.16 × 10(7) L mol(−1)), and the main cause of binding was identified as being due to hydrophobic forces. In addition to the enzyme activity being dose dependent, it was also found that core–shell structures caused an enhancement in activity. Since binary QDs like CdSe also show a change in the lysozyme enzyme activity, therefore, a clear differential between binary and ternary QDs was required to be established which clearly revealed the relevance of surface chemistry on the QD–lysozyme interaction. |
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