Biomimetic protein-harpooning surfaces
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Research Letter
Biomimetic protein-harpooning surfaces G. M. L. Messina, Laboratory for Molecular Surfaces and Nanotechnology (LAMSUN), Department of Chemical Sciences, University of Catania and CSGI, Viale A. Doria 6, Catania 95125, Italy C. Bonaccorso and A. Rapisarda, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania 95125, Italy B. Castroflorio, Laboratory for Molecular Surfaces and Nanotechnology (LAMSUN), Department of Chemical Sciences, University of Catania and CSGI, Viale A. Doria 6, Catania 95125, Italy D. Sciotto, Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania 95125, Italy G. Marletta, Laboratory for Molecular Surfaces and Nanotechnology (LAMSUN), Department of Chemical Sciences, University of Catania and CSGI, Viale A. Doria 6, Catania 95125, Italy Address all correspondence to G. M. L. Messina at [email protected] and C. Bonaccorso at [email protected] (Received 17 January 2018; accepted 26 March 2018)
Abstract Properly driving protein interactions with solid surfaces play a very important role in many natural processes, stimulating a great interest for the design of new biomaterials and medical devices. Despite the progress in this field, many further upgrades have to be achieved to better exploit the protein driving, in terms of control of amounts and conformation of the adsorbing proteins. In this paper, new biocompatible amino acid–calix[4]crown-5 bilayers were built as nano-templating surfaces, hosting a controlled number of anchoring sites, able to immobilize proteins in well-defined quantity, and the evaluated footprint data support the idea of oriented protein on analyzed substrates. The efficiency of the setup was tested for the particular case of antibacterial lysozyme adsorption on biocompatible surfaces.
Introduction Specific anchoring of proteins at solid/liquid interface plays an important role in various biologic processes, including the development of tissue engineering substrates, biomolecule recognition, antibacterial surfaces, etc.[1–7] Surface-bound host–guest assemblies, consisting of amino acid–calix[4]crown-5 (calixarenes) bilayers, have been shown to be able to drive the protein organization and dynamics at interfaces, including their packing, orientation state, native and denatured state, aggregation propensity, and, in turn, their global biologic response.[8–13] The calixarenes, thanks to their synthetic accessibility and versatility, have gained attention for a wide range of applications in chemical, analytical, and engineering materials fields.[14, 15] Recently, we have exploited calixarenes for molecular recognition and self-assembly,[16, 17] reversible supramolecular hydrogels,[18] and as catalysts.[19] In this paper, we propose a new concept of nano-structured surfaces able to “harpoon” biomolecules, including simple amino acids and a model protein, in a controlled way, based on the templating properties of a new calix[4]arene-crown-5 (TCC5), which is covalently anchored onto gold surfaces, forming uniform
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