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

The team at the University of Tokyo used their DAWN detector in conjunction with their Shodex HPLC system to find the molar mass of their T.th cpn/CdS nanoparticle inclusion complex. These results demonstrate that T.th cpn within the protein-nanoparticle complex preserves its own structural identity, without formation of higher aggregates or dissociation into protein subunits. They further report that GroEL and T.th cpn can also enfold CdS semiconductor nanoparticles, giving them high thermal and chemical stability in aqueous media. Such biological mechanisms integrated into materials science may open a door to conceptually new bioresponsive devices. For information on specifics on their MALS data, please see the Supplementary Information for this publication.

Ishii, D.; Kinbara, K.; Ishida, Y.; Ishii, N.; Okochi, M.; Yohda, M.; Aida, T. Nature  2003, 423, 628-632. doi:10.1038/nature01723