Facile Glycoenzyme Wiring to Electrode Supports by Redox-Active Biosupramolecular Glue

DIEGO PALLAROLA; NURIA QUERALTO; WOLFGANG KNOLL; OMAR AZZARONI; FERNANDO BATTAGLINI

CHEMISTRY-A EUROPEAN JOURNAL

WILEY-V C H VERLAG GMBH

Año: 2010 vol. 16 p. 13970 - 13975

0947-6539

The integration of redox glycoenzymes on conductive supports plays a pivotal role in the successful design of bioelectronic platforms, including, among others, biosensors or biofuel cells. Recognition-directed biosupramolecular assembly emerged as an interesting and attractive alternative due to its simplicity and versatility, without introducing chemical modifications to the enzyme. Concanavalin A (Con A), the best studied of the lectins exists as a tetramer with a molecular mass of 104 KDa at neutral pH. Each Con A monomer contains one carbohydrate binding site (specific to a-d-mannose and a-d-glucose), allowing the supramolecular conjugation of the glycoenzyme through its carbohydrate moiety. By incorporating predesigned redox centers into the Con A molecules we were able to create biorecognizable platforms to enable the spontaneous assembly and electrical wiring of glycoenzymes onto electrodes. The redox tagged Con A layer acts not only as a “biosupramolecular glue” to facilitate the robust and easy attachment of the enzyme without affecting its catalytic activity but also as an electron-conducting phase to enable the electrical communication between the prosthetic groups of the enzymes and the electrode support.