Crystalline bacterial cell surface layer (S-layer) proteins are one of the most abundant biopolymers on earth, and form the outermost cell envelope component in a broad range of bacteria and archaea. These S-layer protein lattices represent the simplest biological membranes developed during evolution. S-layer lattices are highly porous protein mesh works with unit cell sizes in the range of 3 to 30 nm, and thicknesses of ∼10 nm. But, one of the key features of S-layer proteins is their intrinsic capability to form self-assembled mono- or double layers in suspension, at solid supports, the air-water interface, planar lipid films, liposomes, nanocapsules, and nano particles.
S-layer proteins have attracted much attention in the literature recently since the reassembly process is entropy-driven and a fascinating example of matrix assembly following a multistage, non-classical pathway. While the formation of extended S-layer protein monolayers is usually in the focus of current research and developments in the life and non-life sciences, S-layer proteins are also able to form more uncommon morphologies (with respect to other biological model systems) such as tubes, ribbons, or extended sheets with a central screw dislocation. In addition, the formation of hollow S-layer protein cages allows to extend the morphogenetic potential of S-layer protein self-assembly into the third dimension.
This contribution summarizes the state-of-the art in the reassembly of S-layer proteins, with a special focus on the uncommon morphologies and the formation of closed three-dimensional S-layer architectures.
Acknowledgements:The Air Force Office of Scientific Research (AFOSR) (Agreement Awards FA9550-12-1-0274 and FA9550-10-1-0223), and the Erwin Schrödinger Society for Nanobiosciences, Vienna, Austria, funded part of this work.
University of Natural Resources and Life Sciences
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