Developing generic strategies for building adaptable or multi-functional bio-platforms is challenging, in particular because protein immobilization onto surfaces often causes loss of protein function and multi-functionality usually necessitates specific combinations of heterogeneous elements. Here we introduce a generic, modular bio-platform construction strategy that uses cage-like supramolecular multi-enzyme complexes as highly adaptable building blocks immobilized directly and non-covalently on graphene. Thermoplasma acidophilum dihydrolipoyl acyltransferase (E2) supramolecular complexes organize as a monolayer or can be controllably transferred onto graphene, preserving their supramolecular form with specific molecular recognition capability and capacity for engineering multi-functionality. This E2-graphene platform can bind enzymes (here, E1, E2’s physiological partner) without loss of enzyme function; in this test case, E1 catalytic activity was detected on E2-graphene over six orders of magnitude in substrate concentration. The E2-graphene platform can be multiplexed via patterned co-transfer of differently modified E2 complexes. As the E2 complexes are robust and highly customizable, E2-graphene is a platform onto which multiple functionalities can be built.
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- Department of Chemistry - Professor
- Institute for Sustainable Energy and the Environment
- Centre for Sustainable and Circular Technologies (CSCT)
- EPSRC Centre for Doctoral Training in Statistical Applied Mathematics (SAMBa)
- Water Innovation and Research Centre (WIRC)
- Centre for Nanoscience and Nanotechnology
- Centre for Biosensors, Bioelectronics and Biodevices (C3Bio)
Person: Research & Teaching