Chaperonin-mediated stabilization and ATP-triggered release of semiconductor nanoparticles

Daisuke Ishii, Kazushi Kinbara, Yasuhiro Ishida, Noriyuki Ishii, Mina Okochi, Masafumi Yohda and Takuzo Aida ()
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Daisuke Ishii: The University of Tokyo
Kazushi Kinbara: The University of Tokyo
Yasuhiro Ishida: The University of Tokyo
Noriyuki Ishii: National Institute of Advanced Industrial Science and Technology
Mina Okochi: Tokyo University of Agriculture and Technology
Masafumi Yohda: Tokyo University of Agriculture and Technology
Takuzo Aida: The University of Tokyo

Nature, 2003, vol. 423, issue 6940, 628-632

Abstract: Abstract Various properties of semiconductor nanoparticles, including photoluminescence and catalytic activity, make these materials attractive for a range of applications1,2. As nanoparticles readily coagulate and so lose their size-dependent properties, shape-persistent three-dimensional stabilizers that enfold nanoparticles have been exploited3,4,5,6,7,8,9. However, such wrapping approaches also make the nanoparticles insensitive to external stimuli, and so may limit their application. The chaperonin proteins GroEL (from Escherichia coli) and T.th (‘T.th cpn’, from Thermus thermophilus HB8) encapsulate denatured proteins inside a cylindrical cavity; after refolding, the encapsulated proteins are released by the action of ATP inducing a conformational change of the cavity10,11. Here we report that GroEL and T.th cpn can also enfold CdS semiconductor nanoparticles, giving them high thermal and chemical stability in aqueous media. Analogous to the biological function of the chaperonins, the nanoparticles can be readily released from the protein cavities by the action of ATP. We expect that integration of such biological mechanisms into materials science will open a door to conceptually new bioresponsive devices.

Date: 2003
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DOI: 10.1038/nature01663

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