In-capillary self-assembly and proteolytic cleavage of polyhistidine peptide capped quantum dots |
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Authors: | Jianhao Wang Jingyan Li Jinchen Li Feifei Liu Xiang Zhou Yi Yao Cheli Wang Lin Qiu Pengju Jiang |
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Institution: | 1. School of Pharmaceutical Engineering and Life Science, Changzhou University, Changzhou, Jiangsu, 213164, China;2. State Key Laboratory of Pharmaceutical Biotechnology, Nanjing, Jiangsu, People''s Republic of China;3. Changzhou Qianhong Bio-pharma Co. Ltd, Changzhou 213164, Jiangsu, People''s Republic of China |
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Abstract: | A new method using fluorescence coupled capillary electrophoresis (CE-FL) for monitoring self-assembly and proteolytic cleavage of hexahistidine peptide capped quantum dots (QDs) inside a capillary has been developed in this report. QDs and the ATTO 590-labeled hexahistidine peptide (H6-ATTO) were injected into a capillary, sequentially. Their self-assembly inside the capillary was driven by a metal-affinity force which yielded a new fluorescence signal due to Förster resonance energy transfer (FRET). The highly efficient separation of fluorescent complexes and the FRET process were analyzed using CE-FL. The self-assembly of QDs and biomolecules was found to effectively take place inside the capillary. The kinetics of the assembly was monitored by CE-FL, and the approach was extended to the study of proteolytic cleavage of surface conjugated peptides. Being the first in-depth analysis of in-capillary nanoparticle–biomolecule assembly, the novel approach reported here provides inspiration to the development of QD-based FRET probes for biomedical applications. |
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Keywords: | Fluorescence coupled capillary electrophoresis Quantum dots Fö rster resonance energy transfer Peptide Thrombin |
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