journal article·2014-08-27

Activation of a Biocatalytic Electrode by Removing Glucose Oxidase from the Surface—Application to Signal Triggered Drug Release

Maria Gamella, Nataliia Guz, Shay Mailloux, José M. Pingarrón, Evgeny Katz

Publisher page

Abstract

A biocatalytic electrode activated by pH signals was prepared with a multilayered nanostructured interface including PQQ-dependent glucose dehydrogenase (PQQ-GDH) directly associated with the conducting support and glucose oxidase (GOx) located on the external interface. GOx was immobilized through a pH-signal-cleavable linker composed of an iminobiotin/avidin complex. In the presence of GOx, glucose was intercepted at the external interface and biocatalytically oxidized without current generation, thus keeping the electrode in its nonactive state. When the pH value was lowered from pH 7.5 to 4.5 the iminobiotin/avidin complex was cleaved and GOx was removed from the interface allowing glucose penetration to the electrode surface where it was oxidized by PQQ-GDH yielding a bioelectrocatalytic current, thus switching the electrode to its active state. This process was used to trigger a drug-mimicking release process from another connected electrode. Furthermore, the pH-switchable electrode can be activated by biochemical signals logically processed by biocatalytic systems mimicking various Boolean gates. Therefore, the developed switchable electrode can interface biomolecular computing/sensing systems with drug-release processes.
Source: openalex_inverted_index · Quality: baseline

Research context

OpenAlex topics: Electrochemical sensors and biosensors · Electrochemical Analysis and Applications · Analytical Chemistry and Sensors

SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.

Affiliations

Department of Chemistry and Biomolecular Science, Clarkson University, Potsdam, New York 13699-5810, United States

Department of Analytical Chemistry, Complutense University of Madrid, 28040 Madrid, Spain

Funding

Division of Chemical, Bioengineering, Environmental, and Transport Systems · Ministerio de Economía y Competitividad

References (36)

Show source-provided references
1. Katz E. · Anal. Bioanal. Chem. · 2013 · 405 · 365910.1007/s00216-012-6525-2 ↗
2. MacVittie K. · J. Phys. Chem. C · 2013 · 117 · 2494310.1021/jp409257v ↗
3. Katz E. · J. Mater. Chem. · 2012 · 22 · 817110.1039/c2jm30172e ↗
4. Laocharoensuk R. · J. Am. Chem. Soc. · 2007 · 129 · 777410.1021/ja0729736 ↗
5. Basso C. R. · Electroanalysis · 2013 · 25 · 181810.1002/elan.201300194 ↗
6. Katz E. · Chem.—Eur. J. · 2009 · 15 · 1255410.1002/chem.200902367 ↗
7. Wang J. · Electrochem. Commun. · 2006 · 8 · 110610.1016/j.elecom.2006.04.019 ↗
8. Meredith M. T. · Anal. Chem. · 2011 · 83 · 543610.1021/ac2011087 ↗
9. Germain M. N. · J. Am. Chem. Soc. · 2008 · 130 · 1527210.1021/ja807250b ↗
10. Zhou M. · J. Am. Chem. Soc. · 2010 · 132 · 217210.1021/ja910634e ↗
11. Katz E. · 2002 · 21910.1016/B978-012635490-4/50008-1 ↗
12. Wang J. · Electroanalysis · 2008 · 20 · 61110.1002/elan.200704120 ↗
13. Song S. · J. Phys. Chem. B · 2010 · 114 · 594010.1021/jp1009753 ↗
14. Tam T. K. · Adv. Mater. · 2010 · 22 · 186310.1002/adma.200903610 ↗
15. Hou K. Y. · J. Phys. Chem. B · 2005 · 109 · 952710.1021/jp044948h ↗
16. Zhou J. · ACS Appl. Mater. Interfaces · 2009 · 1 · 14410.1021/am800088d ↗
17. Privman M. · ACS Appl. Mater. Interfaces · 2011 · 3 · 162010.1021/am200165m ↗
18. Ding F. Y. · J. Mater. Chem. B · 2013 · 1 · 172910.1039/c3tb00517h ↗
19. Zhou M. · Angew. Chem., Int. Ed. · 2012 · 51 · 268610.1002/anie.201107068 ↗
20. Rusling J. F. · Bioelectrochemistry · 2009 · 76 · 18910.1016/j.bioelechem.2009.03.011 ↗
21. Liu A. L. · Trac-Trends Anal. Chem. · 2012 · 37 · 10110.1016/j.trac.2012.03.008 ↗
22. Willner I. · Angew. Chem., Int. Ed. · 2000 · 39 · 118010.1002/(SICI)1521-3773(20000403)39:7<1180::AID-ANIE1180>3.0.CO;2-E ↗
23. Walcarius A. · J. Mater. Chem. B · 2013 · 1 · 487810.1039/c3tb20881h ↗
24. Usui K. · Chem. Commun. · 2013 · 49 · 639410.1039/c3cc41632a ↗
25. Bennett K. L. · Protein Sci. · 2000 · 9 · 150310.1110/ps.9.8.1503 ↗
26. Leriche G. · Bioorg. Med. Chem. · 2012 · 20 · 57110.1016/j.bmc.2011.07.048 ↗
27. Katz E. · Chem. Soc. Rev. · 2010 · 39 · 183510.1039/b806038j ↗
28. Strack G. · Chem. Commun. · 2011 · 47 · 766210.1039/c1cc11475a ↗
29. Katz E. · Energy Environ. Sci. · 2013 · 6 · 279110.1039/c3ee42126k ↗
30. Orr G. A. · J. Biol. Chem. · 1981 · 256 · 76110.1016/S0021-9258(19)70041-6 ↗
31. Hecht H. J. · J. Mol. Biol. · 1993 · 229 · 15310.1006/jmbi.1993.1015 ↗
32. Jin Z. · ACS Appl. Mater. Interfaces · 2012 · 4 · 46610.1021/am201578m ↗
33. Mailloux S. · Anal. Bioanal. Chem. · 2014 · 406 · 482510.1007/s00216-014-7936-z ↗
34. Mailloux S. · Analyst · 2014 · 139 · 98210.1039/c3an02162a ↗
35. Mailloux S. · Chem. Commun. · 2013 · 49 · 475510.1039/c3cc42027b ↗
36. Jin Z. · J. Mater. Chem. · 2012 · 22 · 1952310.1039/c2jm32008h ↗