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Int. J. Mol. Sci. 2017, 18(2), 400; doi:10.3390/ijms18020400

In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers

Department of Nanobiotechnology, Institute for Biophysics, University of Natural Resources and Life Sciences Vienna, Muthgasse 11, Vienna 1190, Austria
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Academic Editor: Vince Rotello
Received: 29 November 2016 / Revised: 17 January 2017 / Accepted: 31 January 2017 / Published: 14 February 2017
(This article belongs to the Section Molecular Recognition)
View Full-Text   |   Download PDF [2485 KB, uploaded 14 February 2017]   |  

Abstract

The recombinant bacterial surface layer (S-layer) protein rSbpA of Lysinibacillus sphaericus CCM 2177 is an ideal model system to study non-classical nucleation and growth of protein crystals at surfaces since the recrystallization process may be separated into two distinct steps: (i) adsorption of S-layer protein monomers on silicon surfaces is completed within 5 min and the amount of bound S-layer protein sufficient for the subsequent formation of a closed crystalline monolayer; (ii) the recrystallization process is triggered—after washing away the unbound S-layer protein—by the addition of a CaCl2 containing buffer solution, and completed after approximately 2 h. The entire self-assembly process including the formation of amorphous clusters, the subsequent transformation into crystalline monomolecular arrays, and finally crystal growth into extended lattices was investigated by quartz crystal microbalance with dissipation (QCM-D) and atomic force microscopy (AFM). Moreover, contact angle measurements showed that the surface properties of S-layers change from hydrophilic to hydrophobic as the crystallization proceeds. This two-step approach is new in basic and application driven S-layer research and, most likely, will have advantages for functionalizing surfaces (e.g., by spray-coating) with tailor-made biological sensing layers. View Full-Text
Keywords: S-layer proteins; two-step crystallization; self-assembly kinetics; non-classical crystal growth; Ca2+ binding S-layer proteins; two-step crystallization; self-assembly kinetics; non-classical crystal growth; Ca2+ binding
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Breitwieser, A.; Iturri, J.; Toca-Herrera, J.-L.; Sleytr, U.B.; Pum, D. In Vitro Characterization of the Two-Stage Non-Classical Reassembly Pathway of S-Layers. Int. J. Mol. Sci. 2017, 18, 400.

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