Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots

Liang Zhao; Kerim M. Gattás-Asfura; Jianmin Xu; Ravi A. Patel; Anup Dadlani; Myrna Sillero-Mahinay; Marie Cushmore; Vipin K. Rastogi; Saumil S. Shah; Roger Leblanc

doi:10.1039/c1cc10714c

Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots

Liang Zhao, Kerim M. Gattás-Asfura, Jianmin Xu, Ravi A. Patel, Anup Dadlani, Myrna Sillero-Mahinay, Marie Cushmore, Vipin K. Rastogi, Saumil S. Shah, Roger Leblanc

Chemistry

Research output: Contribution to journal › Article

8 Scopus citations

Abstract

A direct conjugation of organophosphorus acid anhydrolase (OPAA) with CdS quantum dots was prepared via arrested precipitation within the enzyme matrix. The bio-conjugate was found not only to retain enzyme conformational structure but also to retain enzyme activity and be effective at detecting diisopropyl fluorophosphate (DFP) at the micro molar level.

Original language	English
Pages (from-to)	7242-7244
Number of pages	3
Journal	Chemical Communications
Volume	47
Issue number	25
DOIs	https://doi.org/10.1039/c1cc10714c
State	Published - Jul 5 2011

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ASJC Scopus subject areas

Metals and Alloys
Materials Chemistry
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
Ceramics and Composites
Catalysis
Chemistry(all)

Cite this

Zhao, L., Gattás-Asfura, K. M., Xu, J., Patel, R. A., Dadlani, A., Sillero-Mahinay, M., Cushmore, M., Rastogi, V. K., Shah, S. S., & Leblanc, R. (2011). Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots. Chemical Communications, 47(25), 7242-7244. https://doi.org/10.1039/c1cc10714c

Organophosphorus acid anhydrolase bio-template for the synthesis of CdS quantum dots. / Zhao, Liang; Gattás-Asfura, Kerim M.; Xu, Jianmin; Patel, Ravi A.; Dadlani, Anup; Sillero-Mahinay, Myrna; Cushmore, Marie; Rastogi, Vipin K.; Shah, Saumil S.; Leblanc, Roger.

In: Chemical Communications, Vol. 47, No. 25, 05.07.2011, p. 7242-7244.

Research output: Contribution to journal › Article

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10.1039/c1cc10714c