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단백질 커뮤니케이션 그룹
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Multivalent-Interaction-Driven Assembly of Discrete, Flexible, and Asymmetric Supramolecular Protein Nano-Prisms

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Title
Multivalent-Interaction-Driven Assembly of Discrete, Flexible, and Asymmetric Supramolecular Protein Nano-Prisms
Author(s)
Suyeong Han; Yu-na Kim; Gyunghee Jo; Young Eun Kim; Ho Min Kim; Jeong-Mo Choi; Yongwon Jung
Subject
multivalent interaction, ; protein assembly, ; protein design, ; protein engineering, ; protein-protein interactions
Publication Date
2020-12
Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, v.59, no.51, pp.23244 - 23251
Publisher
WILEY-V C H VERLAG GMBH
Abstract
2020 Wiley-VCH GmbH. 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
URI
https://pr.ibs.re.kr/handle/8788114/7520
DOI
10.1002/anie.202010054
ISSN
1433-7851
Appears in Collections:
Pioneer Research Center for Biomolecular and Cellular Structure(바이오분자 및 세포구조 연구단) > Protein Communication Group(단백질 커뮤니케이션 그룹) > 1. Journal Papers (저널논문)
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