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Int. J. Mol. Sci. 2013, 14(2), 2484-2501; doi:10.3390/ijms14022484
Review
S-Layer Protein Self-Assembly
Department of Nanobiotechnology, Institute for Biophysics, University of Natural Resources and Life Science, Vienna, Muthgasse 11, Vienna 1190, Austria
* Author to whom correspondence should be addressed.
Received: 14 December 2012; in revised form: 14 January 2013 / Accepted: 16 January 2013 / Published: 25 January 2013
(This article belongs to the Special Issue Molecular Self-Assembly 2012)
Abstract: Crystalline S(urface)-layers are the most commonly observed cell surface structures in prokaryotic organisms (bacteria and archaea). S-layers are highly porous protein meshworks with unit cell sizes in the range of 3 to 30 nm, and thicknesses of ~10 nm. One of the key features of S-layer proteins is their intrinsic capability to form self-assembled mono- or double layers in solution, and at interfaces. Basic research on S-layer proteins laid foundation to make use of the unique self-assembly properties of native and, in particular, genetically functionalized S-layer protein lattices, in a broad range of applications in the life and non-life sciences. This contribution briefly summarizes the knowledge about structure, genetics, chemistry, morphogenesis, and function of S-layer proteins and pays particular attention to the self-assembly in solution, and at differently functionalized solid supports.
Keywords: S-layer; self-assembly; fusion protein; surface functionalization; nanobiotechnology
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MDPI and ACS Style
Pum, D.; Toca-Herrera, J.L.; Sleytr, U.B. S-Layer Protein Self-Assembly. Int. J. Mol. Sci. 2013, 14, 2484-2501.
AMA StylePum D, Toca-Herrera JL, Sleytr UB. S-Layer Protein Self-Assembly. International Journal of Molecular Sciences. 2013; 14(2):2484-2501.
Chicago/Turabian StylePum, Dietmar; Toca-Herrera, Jose L.; Sleytr, Uwe B. 2013. "S-Layer Protein Self-Assembly." Int. J. Mol. Sci. 14, no. 2: 2484-2501.
Int. J. Mol. Sci.
EISSN 1422-0067
Published by MDPI AG, Basel, Switzerland
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