The Effect of Amino–Phosphate Interactions on the Biosensing Performance of Enzymatic Graphene Field-Effect Transistors

Gonzalo Eduardo Fenoy, Esteban Piccinini, Wolfgang Knoll, Waldemar Marmisollé, Omar Azzaroni

Research output: Contribution to journalArticlepeer-review

Abstract

The interaction between polyamines and phosphate species is found in a wide range of biological and abiotic systems, yielding crucial consequences that range from the formation of supramolecular colloids to structure determination. In this work, the occurrence of phosphate–amino interactions is evidenced from changes in the electronic response of graphene field effect transistors (gFETs). First, the surface of the transistors is modified with poly(allylamine), and the effect of phosphate binding on the transfer characteristics is interpreted in terms of its impact on the surface charge density. The electronic response of the polyamine-functionalized gFETs is shown to be sensitive to the presence of different phosphate anions, such as orthophosphate, adenosine triphosphate, and tripolyphosphate, and a simple binding model is developed to explain the dependence of the shift of the Dirac point potential on the phosphate species concentration. Afterward, the impact of phosphate–amino interactions on the immobilization of enzymes to polyamine-modified graphene surfaces is investigated, and a decrease in the amount of anchored enzyme as the phosphate concentration increases is found. Finally, multilayer polyamine-urease biosensors are fabricated while increasing the phosphate concentration in the enzyme solution, and the sensing properties of the gFETs toward urea are evaluated. It is found that the presence of simple phosphate anions alters the nanoarchitecture of the polyelectrolyte–urease assemblies, with direct implications on urea sensing.
Original languageEnglish
Pages (from-to)13820-13828
Number of pages9
JournalAnalytical Chemistry
Volume94
Issue number40
DOIs
Publication statusPublished - 2022

Research Field

  • Biosensor Technologies

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