Metallization and investigation of electrical properties of<i>in vitro</i>recrystallized mSbsC-eGFP assemblies

Korkmaz, Nuriye; Börrnert, Felix; Köhler, Denny; Mendes, Rafael G.; Bachmatiuk, Alicja; Rümmeli, Mark H.; Büchner, B.; Eng, Lukas M.; Rödel, Gerhard

doi:10.1088/0957-4484/22/37/375606

Cited by 8 publications

(6 citation statements)

References 37 publications

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“…In this regard, the addition of his-tags to SLPs improves their Ni-chelating capacity, converting the recombinant proteins into attractive self-assembling biological templates for the fabrication of metal nanoclusters and construction of nanomaterials [55,56,73]. This strategy has also been used for the modification of SLPs from Caulobacter crescentus, for the purpose of removing cadmium from water [57].…”

Section: Applications In Bioelectronicsmentioning

confidence: 99%

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Mobili

2013

IJBCRR

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Surface-layers (S-layers) are macromolecular paracrystalline arrays of proteins or glycoproteins that can self-assemble into 2-dimensional semi-permeable meshworks to overlay the cell surface of many bacteria and archaea. They usually assemble into lattices with oblique, square or hexagonal symmetry and serve as an interface between the bacterial cell and the environment. Isolated S-layers can recrystallize into two-dimensional regular arrays in suspension or on various surfaces, thus being an appropriate material for several bionanotechnological purposes. Promising applications of S-layers include their use as biotemplates for the capture of metal ions or the synthesis of metal nanoclusters. Research ArticleInternational Journal of Biochemistry Research & Review, 3(1): 39-62, 2013 40 Considering the use of S-layers as biotemplates for the organization of metal ions or metallic nanoclusters, research on potential of surface layer proteins (SLP) and metals can be understood as an interdisciplinary field, in which different biophysical techniques supply complementary information. In this review, we discuss the SLP as native or engineered "bottom-up" building blocks for metal immobilization structures. We also describe the biophysical techniques used to analyze metal binding properties as well as the information obtained from the investigation of these structures.

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Section: Applications In Bioelectronicsmentioning

confidence: 99%

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Mobili

2013

IJBCRR

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“…[11][12][13] Various assemblies of S-layer proteins can serve as templates to grow other extended nanostructures such as superlattices of metallic clusters. 11,14,15 Tubular structures are also found to form in self-assembly of macromolecules that are usually amphiphilic. 2,[16][17][18][19][20][21][22][23][24][25][26] The location of hydrophobic and hydrophilic groups and other non-covalent interaction sites results in the formation of tubes.…”

Section: 4mentioning

confidence: 99%

Self-assembly of artificial microtubules

2012

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Understanding the complex self-assembly of biomacromolecules is a major outstanding question. Microtubules are one example of a biopolymer that possesses characteristics quite distinct from standard synthetic polymers that are derived from its hierarchical structure. In order to understand how to design and build artificial polymers that possess features similar to those of microtubules, we have initially studied the self-assembly of model monomers into a tubule geometry. Our model monomer has a wedge shape with lateral and vertical binding sites that are designed to form tubules. We used molecular dynamics simulations to study the assembly process for a range of binding site interaction strengths. In addition to determining the optimal regime for obtaining tubules, we have calculated a diagram of the structures that form over a wide range of interaction strengths. Unexpectedly, we find that the helical tubules form, even though the monomer geometry is designed for nonhelical tubules. We present the detailed dynamics of the tubule self-assembly process and show that the interaction strengths must be in a limited range to allow rearrangement within clusters. We extended previous theoretical methods to treat our system and to calculate the boundaries between different structures in the diagram.

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“…Actin filaments which are cytoskeletal units of eukaryotic cells require cations to form functional actin filaments from monomeric units in vivo and in vitro . Various biological molecules such as DNA, bacterial surface layer proteins (S‐layers), and microtubules have been isolated and investigated for their potential application in bottom‐up manufacturing. Ions play an important role in self‐assembly of such nanobiotemplates as well.…”

Section: Introductionmentioning

confidence: 99%

Trivalent Cation Induced Bundle Formation of Filamentous fd Phages

Zirpel

Park

2015

Macromol. Biosci.

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Bacteriophages are filamentous polyelectrolyte viral rods infecting only bacteria. In this study, we investigate the bundle formation of fd phages with trivalent cations having different ionic radii (Al(3+) , La(3+) and Y(3+) ) at various phage and counterion concentrations, and at varying bundling times. Aggregated phage bundles were detected at relatively low trivalent counterion concentrations (1 mM). Although 10 mM and 100 mM Y(3+) and La(3+) treatments formed larger and more intertwined phage bundles, Al(3+) and Fe(3+) treatments lead to the formation of networking filaments. Energy dispersive X-ray spectroscopy (EDX) analyses confirmed the presence of C, N and O peaks on densely packed phage bundles. Immunofluorescence labelling and ELISA analyses with anti-p8 antibodies showed the presence of phage filaments after bundling.

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Metallization and investigation of electrical properties ofin vitrorecrystallized mSbsC-eGFP assemblies

Cited by 8 publications

References 37 publications

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Biophysical Methods for the Elucidation of the S-Layer Proteins/Metal Interaction

Self-assembly of artificial microtubules

Trivalent Cation Induced Bundle Formation of Filamentous fd Phages

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