Self-assembly of phosphorylated peptide driven by Dy3+ |
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| Institution: | 1. CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;2. University of Chinese Academy of Sciences, Beijing 100049, China;3. Zhang Dayu School of Chemistry, Dalian University of Technology, Dalian 116024, China;1. Shanghai Key Laboratory of Multiphase Materials Chemical Engineering, School of Chemical Engineering, East China University of Science and Technology, Shanghai 200237, China;2. State Key Laboratory of Chemical Engineering, School of Chemical Engineering, East China University of Science and Technology, Shanghai 200237, China;1. School of Petrochemical Engineering, Changzhou University, Changzhou 213164, China;2. Department of Chemistry, Maynooth University, National University of Ireland, Maynooth, Co. Kildare, Ireland;3. State Key Laboratory of Analytical Chemistry for Life Science, Jiangsu Key Laboratory of Advanced Organic Materials, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China;1. State Key Laboratory of Elemento-Organic Chemistry, Tianjin Key Laboratory of Biosensing and Molecular Recognition, Frontiers Science Center for New Organic Matter, College of Chemistry, Nankai University, Tianjin 300071, China;2. Haihe Laboratory of Sustainable Chemical Transformation, Tianjin 300192, China;1. Chongqing Key Laboratory of Natural Product Synthesis and Drug Research, Innovative Drug Research Center, School of Pharmaceutical Sciences, Chongqing University, Chongqing 401331, China;2. Shenzhen Innovation Center for Small Molecule Drug Discovery Co., Ltd., Shenzhen 518110, China;3. Chemical Biology Research Center, School of Pharmaceutical Sciences, Chongqing University, Chongqing 401331, China;4. Key Laboratory of Biorheological Science and Technology, Ministry of Education, College of Bioengineering, Chongqing University, Chongqing 400044, China;5. Beijing National Laboratory for Molecular Sciences, Beijing 100190, China;1. School of Biomedical Engineering, Dalian University of Technology, Dalian 116024, China;2. CAS Key Laboratory of Separation Science for Analytical Chemistry, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian 116023, China;3. College of Chemistry and Chemical Engineering, Wuhan Textile University, Wuhan 430200, China;1. Medical College, Guizhou University, Guiyang 550000, China;2. Department of Orthopedics, Guizhou Provincial People''s Hospital, Guiyang 550000, China;3. Department of Orthopaedics, The Affiliated Hospital of Guizhou Medical University, Guiyang 550000, China |
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| Abstract: | Nature chooses phosphorylation as a key modification to modulate and program the functions of proteins. Various phosphorylated peptides (PPs) have been widely identified and investigated by biologists, but the possibility that PPs could become a building unit for artificial materials is neglected. Here we report for the first time a supramolecular assembly of PPs with the assistance of dysprosium ions (Dy3+). Dy3+ bridges multiple phosphate groups in double-phosphorylated peptides (di-PPs), and braid these peptide chains into nanofibers. The assembly occurs inside nanochannels and blocks the channels, leading to prominent “ON–OFF” switching in transmembrane ionic current. The di-PPs’ assembling process could be dynamically regulated by the addition or deletion of phosphate groups under the control of kinases or phosphatases. This study proves the huge potential of PPs being utilized as materials via self-assembling, which will promote the design of novel bio-inspired artificial materials and devices. |
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