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최형주Hyeong Joo Choi
KAIST
Angew. Chem.-Int. Edit., First published: 30 July 2018 | https://doi.org/10.1002/anie.201805749
Fabrication of Oligomeric Avidin Scaffolds for Valency‐Controlled Surface Display of Functional Ligands
Hye Ryeon Yoona,†, Hyeongjoo Choia,†, Yoon-Aa Choib,†, Jung A Kimc, Juyeon Jungb,d,e, Ho Min Kimf, and Yongwon Junga,*
aDepartment of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141 (Korea)
bBionano Health Guard Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141 (Korea)
cGraduate School of Nanoscience and Technology, KAIST
dHazards Monitoring Bionano Research Center, KRIBB, Daejeon 34141 (Korea)
eNanobiotechnology Major, KRIBB School of Engineering, UST, Daejeon 34113 (Korea)
fGraduate School of Medical Science and Engineering, KAIST
†These authors contributed equally.
*To whom correspondence may be addressed.
aDepartment of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141 (Korea)
bBionano Health Guard Research Center, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141 (Korea)
cGraduate School of Nanoscience and Technology, KAIST
dHazards Monitoring Bionano Research Center, KRIBB, Daejeon 34141 (Korea)
eNanobiotechnology Major, KRIBB School of Engineering, UST, Daejeon 34113 (Korea)
fGraduate School of Medical Science and Engineering, KAIST
†These authors contributed equally.
*To whom correspondence may be addressed.
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. Here, we fabricated a series of new oligomeric avidin proteins 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: multivalency, avidin, surface display, ligand, protein engineering
Keywords: multivalency, avidin, surface display, ligand, protein engineering
논문정보
- Research article
- 2018년 07월 (BRIC 등록일 2018-08-27)
- 국내 연구진
- 바이오·의료융합 > 바이오센싱 및 나노바이오물질
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