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Biomimetic protein-harpooning surfaces

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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.

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Acknowledgments

G. M. L. Messina acknowledges the financial support by FIRB 2013—Future in Research (MIUR, Rome). C. Bonaccorso acknowledges the University of Catania for a post-doctoral Fellowship. G. Marletta acknowledges the partial financial support from FIR 2014 (University of Catania).

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Authors and Affiliations

  1. Laboratory for Molecular Surfaces and Nanotechnology (LAMSUN), Department of Chemical Sciences, University of Catania and CSGI, Viale A. Doria 6, Catania, 95125, Italy

    G. M. L. Messina, B. Castroflorio & G. Marietta

  2. Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania, 95125, Italy

    C. Bonaccorso, A. Rapisarda & D. Sciotto

Authors
  1. G. M. L. Messina
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  2. C. Bonaccorso
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  3. A. Rapisarda
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  4. B. Castroflorio
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  5. D. Sciotto
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  6. G. Marietta
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Corresponding authors

Correspondence to G. M. L. Messina or C. Bonaccorso.

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The supplementary material for this article can be found at https://doi.org/10.1557/mrc.2018.54

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Messina, G.M.L., Bonaccorso, C., Rapisarda, A. et al. Biomimetic protein-harpooning surfaces. MRS Communications 8, 241–247 (2018). https://doi.org/10.1557/mrc.2018.54

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