pH-Induced conformational changes of BSA in fluorescent AuNCs@BSA and its effects on NCs emission |
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| Institution: | 1. State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun 130012, PR China;2. College of Chemical & Pharmaceutical Engineering, Jilin Institute of Chemical Technology, Jilin City 132022, China;3. School of Pharmaceutical Sciences, Jilin University, Changchun 130033, China;1. Department of Chemistry, Shiraz University, Shiraz, Iran;2. Faculty of Science, Hormozgan University, Bandar Abbas, Iran;1. School of the Environment and Safety Engineering, Jiangsu University, Zhenjiang 212013, China;2. School of Pharmacy, Jiangsu University, Zhenjiang 212013, China;3. State Key Laboratory of Environmental Chemistry and Ecotoxicology, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, P. O. Box 2871, Beijing 100085, China;1. State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China;2. Key Laboratory of Photochemistry, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China;1. Key Laboratory of Grain and Oil Processing of Jilin Province, Jilin Business and Technology College, No. 4728, Xian Road, Changchun 130012, China;2. State Key Laboratory of Supramolecular Structure and Materials, Jilin University, No. 2699, Qianjin Street, Changchun 130012, China;3. Shenyang Aircraft Corporation, No. 1, Lingbei Street, Shenyang 110034, China;1. Dipartimento di Fisica e Chimica, Università di Palermo, Viale delle Scienze, Building 18, 90100, Palermo, Italy;2. Istituto di Biofisica, Consiglio Nazionale delle Ricerche, Via U. La Malfa 153, 90100, Palermo, Italy;3. Istituto di Biomedicina e Immunologia Molecolare, Consiglio Nazionale delle Ricerche, Via U. La Malfa 153, 90100, Palermo, Italy |
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| Abstract: | We investigated the pH-induced fluorescence changes of BSA-protected gold nanoclusters, Au16NCs@BSA, and the corresponding conformational changes of ligand protein by fluorescence, circular dichrosim (CD) and IR spectral measurements. The studies presented here demonstrated that BSA in AuNCs@BSA underwent identifiable conformational changes on both the secondary and the tertiary structure levels. The results of CD and IR interpreted the significant change of second structures at extreme acidity and alkaline, where more unordered structures were gained. Of note was that the extreme alkaline (pH = 11.43) induced the changes from exposed to buried α-helices, which was different from the pH-induced structural changes of BSA. In addition, the large fluorescence intensity gap of tryptophan between AuNCs@BSA and native BSA indicated efficient energy transfer took place between BSA and AuNCs, implying that the gold core resided near tryptophan in BSA. |
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