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Fabrication of Oligomeric Avidin Scaffolds for Valency‐Controlled Surface Display of Functional Ligands
Authors:Dr Hye Ryeon Yoon  Hyeongjoo Choi  Dr Yoon‐Aa Choi  Dr Jung A Kim  Dr Juyeon Jung  Prof Ho Min Kim  Prof Yongwon Jung
Institution:1. Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, Korea;2. Bionano Health Guard Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon, Korea;3. Graduate School of Nanoscience and Technology, KAIST, Korea;4. Hazards Monitoring Bionano Research Center, KRIBB, Daejeon, Korea;5. Nanobiotechnology Major, KRIBB School of Engineering, UST, Daejeon, Korea;6. Graduate School of Medical Science and Engineering, KAIST, Korea
Abstract:Multivalent surface display of biomolecules is crucial to study and utilize multivalent biological interactions. However, precise valency control of surface‐displayed ligands remains extremely difficult. Now a series of new oligomeric avidin proteins were fabricated that allow facile control of surface multivalency of biotinylated ligands. Naturally dimeric rhizavidin (RA) was engineered to form a mixture of oligomeric avidin assemblies, and discrete RA oligomers from the dimer to octamer of RA, were homogeneously prepared. These oligomeric avidins are in polygonal forms with expected numbers of stable biotin binding sites. Upon immobilization on low‐density biotin‐coated gold surfaces, RA dimer, trimer, and tetramer scaffolds provided accurate mean residual valencies of 2, 3, and 4, respectively, for biotinylated proteins. Valency‐controlled display of antibody binding protein G on these RA surfaces showed clear valency‐dependent enhancement of antibody capturing stability.
Keywords:avidin  multivalency  protein engineering  rhizavidin  surface display
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