Spectroscopic and Isothermal Titration Calorimetry Studies of Binding Interactions Between Carbon Nanodots and Serum Albumins |
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| Authors: | Chang-Qing Xiao Lu Lai Li Zhang Song-Yang Wang Sui Yuan Zi-Qiang Xu Yi Liu |
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| Institution: | 1.Hubei Key Laboratory of Purification and Application of Plant Anticancer Active Ingredients, School of Chemistry and Life Sciences,Hubei University of Education,Wuhan,People’s Republic of China;2.State Key Laboratory of Virology & Key Laboratory of Analytical Chemistry for Biology and Medicine (MOE), College of Chemistry and Molecular Sciences,Wuhan University,Wuhan,People’s Republic of China;3.College of Chemistry and Environmental Engineering,Yangtze University,Jingzhou,People’s Republic of China;4.Hubei Collaborative Innovation Center for Advanced Organic Chemical Materials, Ministry-of-Education Key Laboratory for the Green Preparation and Application of Functional Materials, Hubei Key Laboratory of Polymer Materials, School of Materials Science & Engineering,Hubei University,Wuhan,People’s Republic of China |
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| Abstract: | Carbon nanodots (C-dots) have attracted great attention as a new class of luminescent nanomaterials. In order to better understand the basic behavior of C-dots in biological systems, the binding characteristics of C-dots with bovine serum albumin (BSA) and human serum albumin (HSA) were investigated using spectroscopic approaches and isothermal titration calorimetry at pH 7.4. We found that the intrinsic fluorescence of BSA and HSA was quenched by the C-dots with a dynamic quenching mode. It was proved that the C-dots had little influence on the conformation of BSA and HSA by their UV–vis and circular dichroism spectra. Some important thermodynamic parameters were calculated, and the positive values of ΔH° and ΔS° indicate that the binding process was endothermic, and that the interaction was driven by favorable entropy and unfavorable enthalpy. It also showed that the hydrophobic force played a major role in the binding process. |
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