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Bernhard Schuster

Publications and source records attributed to Bernhard Schuster.

7 recordsLinked to original sources

S-Layers as a basic building block in a molecular construction kit.

Crystalline arrays of protein or glycoprotein subunits forming surface layers (S-layers) are the most common outermost envelope components of prokaryotic organisms (archaea and bacteria). The wealth of information on the structure, chemistry, genetics, morphogenesis, and function of S-layers has revealed a broad application potential. As S-layers are periodic structures, they exhibit identical physicochemical properties for each molecular unit down to the subnanometer level and possess pores of identical size and morphology. Many applications of S-layers in nanobiotechnology depend on the ability of isolated subunits to recrystallize into monomolecular lattices in suspension or on suitable surfaces and interfaces. S-Layer lattices can be exploited as scaffolding and patterning elements for generating more complex supramolecular assemblies and structures, as required for life and nonlife science applications.

Animals↗

S-layers as patterning elements for application in nanobiotechnology.

Two-dimensional bacterial cell surface layer protein crystals (S-layers) are the most commonly observed cell surface structure in bacteria and archaea. Isolated S-layer proteins have the intrinsic tendency to self-assemble into crystalline arrays in suspension and on various interfaces. Basic research on the structure, genetics, chemistry, morphogenesis and function of S-layers has led to a broad spectrum of applications in nanotechnology and biomimetics. The possibility to change the properties of S-layer proteins by genetic engineering opens new ways for tuning their functional and structural features. Functionalized S-layer proteins that maintain their ability to self-assemble have led to new affinity matrices, diagnostic tools, vaccines or biocompatible surfaces, as well as to biological templating or specific biomineralisation strategies at surfaces.

Bacterial Proteins↗

Nanotechnology with S-layer proteins.

The cross-fertilization of biology, chemistry, material sciences, and solid-state physics is opening up a great variety of new opportunities for innovation in nanosciences. One of the key challenges is the technological utilization of self-assembly systems wherein molecules spontaneously associate under equilibrium conditions into reproducible supramolecular aggregates. The attractiveness of such processes lies in their capability to build uniform, ultrasmall functional units and the possibility of exploiting such structures at meso- and macroscopic scale for life and nonlife science applications. The use of crystalline bacterial cell-surface proteins (S-layer proteins) provided innovative approaches for the assembly of supramolecular structures and devices with dimensions of a few to tens of nanometers. S-layers have proven to be particularly suited as building blocks in a molecular construction kit involving all major classes of biological molecules. The immobilization of biomolecules in an ordered fashion on solid substrates and their controlled confinement in definite areas of nanometer dimensions are key requirements for many applications including the development of bioanalytical sensors, biochips, molecular electronics, biocompatible surfaces, and signal processing among functional membranes, cells, and integrated circuits.

Animals↗

Highly robust lipid membranes on crystalline S-layer supports investigated by electrochemical impedance spectroscopy.

In the present work, S-layer supported lipid membranes formed by a modified Langmuir-Blodgett technique were investigated by electrochemical impedance spectroscopy (EIS). Basically two intermediate hydrophilic supports for phospholipid- (DPhyPC) and bipolar tetraetherlipid- (MPL from Thermoplasma acidophilum) membranes have been applied: first, the S-layer protein SbpA isolated from Bacillus sphaericus CCM 2177 recrystallized onto a gold electrode; and second, as a reference support, an S-layer ultrafiltration membrane (SUM), which consists of a microfiltration membrane (MFM) with deposited S-layer carrying cell wall fragments. The electrochemical properties and the stability of DPhyPC and MPL membranes were found to depend on the used support. The specific capacitances were 0.53 and 0.69 microF/cm(2) for DPhyPC bilayers and 0.75 and 0.77 microF/cm(2) for MPL monolayers resting on SbpA and SUM, respectively. Membrane resistances of up to 80 mega Ohm cm(2) were observed for DPhyPC bilayers on SbpA. In addition, membranes supported by SbpA exhibited a remarkable long-term robustness of up to 2 days. The membrane functionality could be demonstrated by reconstitution of membrane-active peptides such as valinomycin and alamethicin. The present results recommend S-layer-supported lipid membranes as promising structures for membrane protein-based biosensor technology.

Alamethicin↗

S-layer proteins as supporting scaffoldings for functional lipid membranes.

A great challenge is the coupling of very sensitive microelectronic devices to wet biological systems in the generation of biomimetic sensors. Lipid membranes on solid supports (electrodes or semiconductors) may become the matrix of future bioelectronic devices probing and controlling biomolecular processes for scientific and technical applications. A sufficient electrical isolation between the coupling region and the surrounding electrolyte is mandatory. An attached lipid membrane with integral natural or designed proteins may be the material of choice if the biological components are kept in a proper environment. To retain the fluidity and stability of the lipid membrane and to provide an ion reservoir and space for bulky integral proteins, a separating layer composed of crystalline arrays of monomolecular proteinaceous subunits, termed S-layer, can be self-assembled on metal or semiconductor surfaces. In this way S-layer-supported lipid membranes are biomimetic structures mimicking the supramolecular principle of archeal cell envelopes. These composite architectures may ascend toward exciting new key devices, particularly in fields of membrane protein-based biosensors or lab-on-a-chip technology.

Bacterial Proteins↗

The effect of hydrostatic pressure on S-layer-supported lipid membranes.

We report on the behavior of unsupported and surface layer (S-layer)-supported lipid membranes at the application of a uniform hydrostatic pressure. At a hydrostatic pressure gradient higher than 6 N/m(2), unsupported lipid membranes, independent from which side pressurized and S-layer-supported lipid membranes pressurized from the lipid-faced side revealed a pronounced increase in capacitance. A maximal hydrostatic pressure gradient of 11.0 N/m(2) resulted in an almost doubling of the capacitance of the (composite) membranes. S-layer-supported lipid membranes showed a hysteresis in the capacitance versus pressure plot, indicating that this composite structure required a certain time to reorient when the pressure gradient acting from the lipid-faced side was balanced. By contrast, the S-layer-supported lipid membrane pressurized from the protein-faced side revealed only a minute increase in capacitance (C/C(0,max)=1.17+/-0.05), reflecting only minor pressure-induced area expansion. In addition, no hysteresis could be observed, indicating that no rearrangement of the composite membrane occurred. The maximal induced tension was with 4.3+/-0.2 mN/m, significantly higher than that of unsupported (2.5+/-0.3 mN/m) and S-layer-supported lipid membranes pressurized from the lipid-faced side (2.6+/-0.1 mN/m).

Bacterial Proteins↗

Single channel recordings of alpha-hemolysin reconstituted in S-layer-supported lipid bilayers.

Previous studies demonstrated that lipid membranes attached to a proteinaceous crystalline surface-layer (S-layer) revealed a prolonged lifetime and showed a reduced tendency to rupture in the presence of membrane active molecules. In addition, comparative studies on folded and S-layer-supported lipid membranes (SsLM) revealed an uniform capacitance of 0.64 +/- 0.04 microF/cm(2) for both composite membranes. In the present study, the feasibility to reconstitute the channel-forming protein alpha-hemolysin (alpha HL) into SsLM at single channel resolution was investigated. Single alpha HL channels could be recorded and the intrinsic properties like unitary conductance, current-voltage characteristics, and closure was found to be similar at both membranes. Thus, the tightly attached S-layer allowed complete reconstitution of alpha HL channels in SsLM.

Bacterial Proteins↗