Abstract
We have created modified protein variants by introducing a non-canonical amino acid p-azido-l-phenylalanine (azF) into defined positions for photochemically-induced covalent attachment to graphene. Attachment of GFP, TEM and cyt b562 proteins was verified through a combination of atomic force and scanning tunnelling microscopy, resistance measurements, Raman data and fluorescence measurements. This method can in principle be extended to any protein which can be engineered in this way without adversely affecting its structural stability.
Highlights
The measurement and control of electron transport through single molecule junctions is an important step in the development of single molecule electronic components and chemical or biochemical sensors.[1,2,3] More recently, due to their inherent molecular recognition properties, protein molecules have become a particular focus.[1]
Using a reprogrammed genetic code we introduce the non-proteinogenic, noncanonical amino acid p-azido-L-phenylalanine into a de ned position in a protein
We have shown experimentally that we can incorporate new chemistry into proteins to enable covalent linkage of protein molecules with graphene
Summary
The measurement and control of electron transport through single molecule junctions is an important step in the development of single molecule electronic components and chemical or biochemical sensors.[1,2,3] More recently, due to their inherent molecular recognition properties, protein molecules have become a particular focus.[1]. Cysteine is still present in many proteins, and needs to undergo additional chemical modi cation to facilitate indirect interfacing with many electronically active non-metallic surfaces, such as graphene. This can result in the loss of intimate electronic coupling between protein and surface. Covalent coupling provides a strong, intimate link between the two systems compared to approaches that require additional steps to attach intermediate moieties such as pyrene.[17,18,19] It allows far more control of position within the protein so as to optimise communication between the protein functional centre and the carbon surface; this is not possible with peptide handles that can only be attached to termini of a protein.[20,21] Aromatic rings can promote surface binding through p stacking so helping to place the nitrene close to the conjugated network
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