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Development of a Hybrid Enzyme-Based Porous Silicon Platform for Chemical Warfare Agent Detection

Published online by Cambridge University Press:  01 February 2011

Sonia E. Létant ,
Bradley R. Hart ,
Staci R. Kane ,
Masood Z. Hadi ,
Sharon J. Shields ,
Tu-Chen Cheng ,
Vipin K. Rastogi ,
J. Del Eckels  and
John G. Reynolds
Sonia E. Létant
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
Bradley R. Hart
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
Staci R. Kane
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
Masood Z. Hadi
Affiliation:
Lockheed Martin Corporation, Sandia National Laboratory, Livermore CA, 94551.
Sharon J. Shields
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
Tu-Chen Cheng
Affiliation:
U. S. Army Edgewood Research, Development, and Engineering Center, Aberdeen, MD 21010.
Vipin K. Rastogi
Affiliation:
U. S. Army Edgewood Research, Development, and Engineering Center, Aberdeen, MD 21010.
J. Del Eckels
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
John G. Reynolds
Affiliation:
Forensic Science Center, University of California, Lawrence Livermore National Laboratory, Livermore, CA 94551.
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Abstract

The goal of our research is to combine porous silicon and enzymes in order to build hybrid platforms for extremely selective chemical sensing applications. For this, a new synthetic route to covalently anchor bio-molecules on photo-luminescent porous silicon (PL PSi) while preserving the optical properties of the matrix was developed. The hydride terminated porous silicon surface was covalently functionalized with t-butyloxycarbonyl protected amine by light-assisted hydrosysilation. Protein cross-linker chemistry was then used to extend the linker and immobilize various enzymes. The glu-coronidase enzyme/p-nitro-phenyl-beta-glucoronide substrate test system provided a proof of concept for an enzyme-based porous silicon detector. The enzymatic activity and the luminescence of the porous silicon platform were both retained after the functionali-zation procedure and, charge transfer between the products of the enzymatic breakdown and the silicon quantum dots was demonstrated. The organophosphorous hydrolase enzyme OPAA was then immobilized and tested on p-nitrophenyl-soman, a surrogate substrate for soman. The production of the hydrolysis product, p-nitrophenol, correlated with the reversible luminescence quenching of the porous silicon matrix demonstrating the relevance of the enzyme-based platform for detection applications. This detection scheme, although indirect, takes advantage of the extreme specificity of enzymes. The approach is general and can be implemented for a series of target molecules.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 828: Symposium A – Semiconductor Materials for Sensing , 2004 , A1.8
Copyright
Copyright © Materials Research Society 2005

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References

REFERENCES

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