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Biomimetic protein-harpooning surfaces

Published online by Cambridge University Press:  06 April 2018

G. M. L. Messina Open the ORCID record for G. M. L. Messina [Opens in a new window] ,
C. Bonaccorso ,
A. Rapisarda ,
B. Castroflorio ,
D. Sciotto  and
G. Marletta
G. M. L. Messina*
Affiliation:
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*
Affiliation:
Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania 95125, Italy
A. Rapisarda
Affiliation:
Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania 95125, Italy
B. Castroflorio
Affiliation:
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
Affiliation:
Department of Chemical Sciences, University of Catania, Viale A. Doria 6, Catania 95125, Italy
G. Marletta
Affiliation:
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 grmessi@unict.it and C. Bonaccorso at bonaccorsoc@gmail.com
Address all correspondence to G. M. L. Messina at grmessi@unict.it and C. Bonaccorso at bonaccorsoc@gmail.com
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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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Type
Research Letters
Information
MRS Communications , Volume 8 , Issue 2 , June 2018 , pp. 241 - 247
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Copyright
Copyright © Materials Research Society 2018 

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