ATP-Responsive Nanoparticles Covered with Biomolecular Machine "Chaperonin GroEL"

Hao K Shen; Kiyoshi Morishita; P K Hashim; Kou Okuro; Daiki Kashiwagi; Ayumi Kimura; Haruaki Yanagisawa; Masahide Kikkawa; Tatsuya Niwa; Hideki Taguchi; Takuzo Aida

doi:10.1002/anie.202304894

ATP-Responsive Nanoparticles Covered with Biomolecular Machine "Chaperonin GroEL"

Angew Chem Int Ed Engl. 2023 Aug 1;62(31):e202304894. doi: 10.1002/anie.202304894. Epub 2023 Jun 22.

Authors

Hao K Shen¹, Kiyoshi Morishita^{1

2}, P K Hashim¹, Kou Okuro³, Daiki Kashiwagi¹, Ayumi Kimura⁴, Haruaki Yanagisawa⁵, Masahide Kikkawa⁵, Tatsuya Niwa⁶, Hideki Taguchi⁶, Takuzo Aida^{1

2}

Affiliations

¹ Department of Chemistry and Biotechnology, School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-8656, Japan.
² RIKEN Center for Emergent Matter Science, 2-1 Hirosawa, Wako, Saitama, 351-0198, Japan.
³ State Key Laboratory of Synthetic Chemistry and Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
⁴ Institute of Engineering Innovation, School of Engineering, The University of Tokyo, 2-11-16 Yayoi, Bunkyo-ku, Tokyo, 113-8656, Japan.
⁵ Department of Cell Biology and Anatomy, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
⁶ Cell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Midori-ku, Yokohama, 266-8501, Japan.

PMID: 37243902
DOI: 10.1002/anie.202304894

Abstract

Herein, we report an ATP-responsive nanoparticle (^GroEL NP) whose surface is fully covered with the biomolecular machine "chaperonin protein GroEL". ^GroEL NP was synthesized by DNA hybridization between a gold NP with DNA strands on its surface and GroEL carrying complementary DNA strands at its apical domains. The unique structure of ^GroEL NP was visualized by transmission electron microscopy including under cryogenic conditions. The immobilized GroEL units retain their machine-like function and enable ^GroEL NP to capture denatured green fluorescent protein and release it in response to ATP. Interestingly, the ATPase activity of ^GroEL NP per GroEL was 4.8 and 4.0 times greater than those of precursor ^cys GroEL and its DNA-functionalized analogue, respectively. Finally, we confirmed that ^GroEL NP could be iteratively extended to double-layered $^{(GroEL)_{2}}$ NP.

Keywords: Biomolecular Machine; GroEL; Host-Guest Chemistry; Nanoparticle; Protein Assembly.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenosine Triphosphate* / metabolism
Chaperonin 60 / chemistry
Chaperonins* / metabolism
Protein Folding

Substances

Chaperonins
Adenosine Triphosphate
Chaperonin 60