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Multivalent-Interaction-Driven Assembly of Discrete,Flexible, and Asymmetric Supramolecular Protein Nano-Prisms |
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| Authors: | Suyeong Han Dr Yu-na Kim Gyunghee Jo Dr Young Eun Kim Prof?Dr Ho Min Kim Dr Jeong-Mo Choi Prof?Dr Yongwon Jung |
| Institution: | 1. Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141 Korea
These authors contributed equally to this work.;2. Biomedical Science and Engineering Interdisciplinary Program, KAIST, Daejeon, 34141 Korea;3. Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141 Korea;4. Graduate School of Medical Science & Engineering, KAIST, Daejeon, 34141 Korea Center for Biomolecular & Cellular Structure, Institute for Basic Science (IBS), Daejeon, 34126 Korea;5. Natural Science Research Institute, KAIST, Daejeon, 34141 Korea |
| Abstract: | Current approaches to design monodisperse protein assemblies require rigid, tight, and symmetric interactions between oligomeric protein units. Herein, we introduce a new multivalent-interaction-driven assembly strategy that allows flexible, spaced, and asymmetric assembly between protein oligomers. We discovered that two polygonal protein oligomers (ranging from triangle to hexagon) dominantly form a discrete and stable two-layered protein prism nanostructure via multivalent interactions between fused binding pairs. We demonstrated that protein nano-prisms with long flexible peptide linkers (over 80 amino acids) between protein oligomer layers could be discretely formed. Oligomers with different structures could also be monodispersely assembled into two-layered but asymmetric protein nano-prisms. Furthermore, producing higher-order architectures with multiple oligomer layers, for example, 3-layered nano-prisms or nanotubes, was also feasible. |
| Keywords: | multivalent interaction protein assembly protein design protein engineering protein–protein interactions |