Universal Biomolecule Binding Interlayers Created by Energetic Ion Bombardment
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Universal Biomolecule Binding Interlayers Created by Energetic Ion Bombardment Prof Marcela M.M. Bilek1, Prof David R. McKenzie1, Dr Daniel V. Bax1,2, Dr Alexey Kondyurin1, Dr Yongbai Yin1, Dr Neil. J. Nosworthy1,3, Ms Stacey Hirsh1, Dr Keith Fisher4, Prof Anthony S. Weiss2 1
School of Physics, University of Sydney, NSW 2006 Australia School of Molecular Biosciences, University of Sydney NSW 2006 Australia 3 School of Medical Sciences, University of Sydney, NSW 2006 Australia 4 School of Chemistry, University of Sydney, NSW 2006 Australia 2
ABSTRACT The ability to strongly attach biomolecules such as enzymes and antibodies to surfaces underpins a host of technologies that are rapidly growing in utility and importance. Such technologies include biosensors for medical and environmental applications and protein or antibody diagnostic arrays for early disease detection. Emerging new applications include continuous flow reactors for enzymatic chemical, textile or biofuels processing and implantable biomaterials that interact with their host via an interfacial layer of active biomolecules. In many of these applications it is desirable to maintain physical properties of an underlying material whilst engineering a surface suitable for attachment of proteins or peptide constructs. Nanoscale polymeric interlayers are attractive for this purpose. We have developed interlayers[1] that form the basis of a new biomolecule binding technology with significant advantages over other currently available methods. The interlayers, created by the ion implantation of polymer like surfaces, achieve covalent immobilization on immersion of the surface in protein solution. The interlayers can be created on any underlying material and ion stitched into its surface. The covalent immobilization of biomolecules from solution is achieved through the action of highly reactive free radicals in the interlayer. In this paper, we present characterisation of the structure and properties of the interlayers and describe a detailed kinetic model for the covalent attachment of protein molecules directly from solution. INTRODUCTION Environmental biosensors[2], antibody microarrays for early and precise disease diagnosis [3]and bio-mimetic surface coatings for medical implants[4, 5] require functional[4, 6] immobilised proteins, such as enzymes and antibodies. The capability to robustly immobilise all proteins expressed in a cell would enable “reverse phase” microarrays [7]. The biological responses to implanted biomedical devices could potentially be controlled with a conformal coverage of bioactive proteins or peptide segments [4, 8-10]. Simple techniques to achieve strong and functional binding[9] that perform well across a wide range of proteins and on a wide range of surfaces are required to facilitate the development of medical and sensing technologies that call for immobilised biomolecules with high functionality. The conformation or shape of a biomolecule is the configuration in space that minimises the energy of the protein and its immediate enviro
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