Hostname: page-component-cd9895bd7-q99xh Total loading time: 0 Render date: 2024-12-27T01:57:51.008Z Has data issue: false hasContentIssue false

Photochemical Enzyme Co-Factor Regeneration: Towards Continuous Glutamate Monitoring with a Sol-Gel Optical Biosensor

Published online by Cambridge University Press:  01 February 2011

Jenna L. Rickus
Affiliation:
Neuroscience IDP, Neuroengineering Program
Allan J. Tobin
Affiliation:
Brain Research Institute
Jeffrey I. Zink
Affiliation:
Department of Chemistry and Biochemistry
Bruce Dunn
Affiliation:
Department of Materials Science and Engineering
Get access

Abstract

Sol-gel encapsulation has recently surfaced as a successful approach to biomolecule immobilization. Proteins, including enzymes, are trapped in the pores of the sol-gel derived glass while retaining their spectroscopic properties and biological activity. Our current work extends the unique capabilities of biomolecule-doped sol-gel materials to the detection of glutamate, the major excitatory neurotransmitter in the central nervous system. We are developing an in vivo fiber optic biosensor for glutamate along with methods to achieve continuous monitoring. In our research to date we have encapsulated GDH in a silica sol-gel film on the tip of an optical fiber. GDH catalyzes the oxidative deamination of glutamate to α-ketoglutarate and the simultaneous reduction of NAD+ to NADH. To quantify the glutamate concentration, we observe the rate of change of NADH fluorescence as a function of time. An important consideration for continuous in vivo monitoring is the incorporation of a selfsustaining NAD+ source. We have adopted a photochemical means of regenerating NAD+ from NADH, by irradiating thionine (3,7-diaminophenothiazin-5-ium) which we incorporate into the sol-gel sensor material. When excited with visible light (λabc∼ 596 nm), thionine undergoes a reaction with NADH resulting in a non-fluorescent form of thionine and NAD+. We have characterized the kinetics of this reaction in the sol-gel matrix, and have shown that the reaction results in regenerated co-factor that is usable by GDH for the oxidation of glutamate.

Type
Research Article
Copyright
Copyright © Materials Research Society 2002

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

[1] Alvarez, N.S. Ortea, P.M. Paneda, A.M. Castanon, M.J.L. Ordieres, A.J.M. and Blanco, P.T. Journal of Electroanalytical Chemistry, 502 (2001) 109117.Google Scholar
[2] Dave, B.C. Dunn, B. Valentine, J.S. and Zink, J.I. Analytical Chemistry, 66 (1994) 1120A1127A.Google Scholar
[3] Dunn, B. and Zink, J.I. Chemistry of Materials, 9 (1997) 22802291.Google Scholar
[4] Pereira, A.C. Fertonani, F.L. Neto, G.d.O. Kubota, L.T. and Yamanaka, H. Talanta, 53 (2001) 801806.Google Scholar
[5] Rickus, J.L. Dunn, B. and Zink, J.I. Optically Based Sol-Gel Biosensor Materials. In Ligler, F. and Taitt, C.R. (Eds.), Optical Biosensors: Present and Future, Elsevier, in press.Google Scholar
[6] Rickus, J.L. Lan, E. Tobin, A.J. Zink, J.I. and Dunn, B. Materials Research Society Fall Meeting, Vol. 662, Materials Research Society, Boston Massachusetts, 2000.Google Scholar
[7] Sharma, A. Spectrochimica Acta, 48 (1992) 647651.Google Scholar
[8] Sharma, A. Spectrochimica Acta, 48A (1992) 893897.Google Scholar
[9] Sharma, A. and Quantrill, N.S.M. Spectrochimica Acta, 50A (1994) 11791193.Google Scholar
[10] Tzang, C.H. Yaun, R. and Yang, M. Biosensors and Bioelectronics, 16 (2001) 211219.Google Scholar