Fluorescence resonance energy transfer by S-layer coupled fluorescence dyes

Weinert, Ulrike; Pollmann, Katrin; Raff, Johannes

doi:10.1016/j.snb.2013.05.051

Cited by 5 publications

(6 citation statements)

References 30 publications

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“…The results showed that at least 20% of the calculated functional groups were modifiable on SlfB. In other work SlfB was modified with FRET-pairs and showed modification rates of only 0.15–0.6 mol dye ∙mol SlfB −1 [15]. Although the reported modification rates are not in conflict with those reported here, they prove the influence of molecule size and charge effects on the modification rates.…”

Section: Resultssupporting

confidence: 54%

“…These properties make S-layer proteins quite interesting for applications in biotechnology and material science. S-layer proteins can be used to cover numerous technical surfaces, thus enabling the introduction of diverse functionalities like sorptive or catalytic properties [11,12], or work as binding matrices for enzymes and fluorescent dyes [13,14,15]. For these approaches, the chemical composition of the proteins is of great interest.…”

Section: Introductionmentioning

confidence: 99%

“…In these studies, the location as well as the amount of the bound molecules was reproducible. In a more recent work, S-layer proteins were modified with two different fluorescent dyes that are able to perform a Foerster resonance energy transfer (FRET) [15]. The fluorescent dyes were also bound to the S-layer proteins by EDC.…”

Section: Introductionmentioning

confidence: 99%

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Synthesis of S-Layer Conjugates and Evaluation of Their Modifiability as a Tool for the Functionalization and Patterning of Technical Surfaces

et al. 2015

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Chemical functional groups of surface layer (S-layer) proteins were chemically modified in order to evaluate the potential of S-layer proteins for the introduction of functional molecules. S-layer proteins are structure proteins that self-assemble into regular arrays on surfaces. One general feature of S-layer proteins is their high amount of carboxylic and amino groups. These groups are potential targets for linking functional molecules, thus producing reactive surfaces. In this work, these groups were conjugated with the amino acid tryptophan. In another approach, SH-groups were chemically inserted in order to extend the spectrum of modifiable groups. The amount of modifiable carboxylic groups was further evaluated by potentiometric titration in order to evaluate the potential efficiency of S-layer proteins to work as matrix for bioconjugations. The results proved that S-layer proteins can work as effective matrices for the conjugation of different molecules. The advantage of using chemical modification methods over genetic methods lies in its versatile usage enabling the attachment of biomolecules, as well as fluorescent dyes and inorganic molecules. Together with their self-assembling properties, S-layer proteins are suitable as targets for bioconjugates, thus enabling a nanostructuring and bio-functionalization of surfaces, which can be used for different applications like biosensors, filter materials, or (bio)catalytic surfaces.

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Section: Resultssupporting

confidence: 54%

Section: Introductionmentioning

confidence: 99%

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Synthesis of S-Layer Conjugates and Evaluation of Their Modifiability as a Tool for the Functionalization and Patterning of Technical Surfaces

et al. 2015

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“…Another alternative is the combination of aptamers with an existing FRET system that is applied to the S-layer surface. As shown in a previous work, Slayer proteins can be functionalized simply with an FRET pair by chemical modification and an FRET can be detected on S-layer protein covered surface [19]. Thereby, S-layer proteins showed no quenching effects to the fluorophores because of their hydrophobic environment.…”

Section: Discussionmentioning

confidence: 61%

“…Furthermore, the molecules are packed within a nanometer range. In a previous work, two different fluorescence dyes, able to perform a Förster resonance energy transfer, were randomly covalently linked to the surface with carbodiimides and gained an energy transfer efficiency of 40% . This fact also proves that molecules are regularly arranged on S‐layer surface despite their unspecific binding procedures by carbodiimides for example.…”

Section: Introductionmentioning

confidence: 79%

S‐layer proteins as an immobilization matrix for aptamers on different sensor surfaces

Weinert

Vogel

Reinemann

et al. 2015

Engineering in Life Sciences

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S-layer proteins provide a biocompatible environment with different kinds of functional groups, perfect for the sequential coupling of any kind of biofunctional molecule. In addition, their nanostructure and their ability to crystallize on surfaces in a nanometer-thick monolayer ensure a regular arrangement of these molecules on solid supports. In this work, a thrombin-binding aptamer and an ofloxacin-binding aptamer were coupled with different chemical crosslinkers to S-layer proteins using them for defined immobilization. S-layer protein monomers and paracrystalline S-layers were successfully modified with the thrombin-binding aptamer. However, S-layer protein monomers were not able to crystallize after aptamer modification and showed no thrombin binding during random surface attachment. In contrast, aptamers linked to an intact S-layer in suspension or an S-layer coating were still functional. The modification rate of S-layers with the thrombin-binding aptamer was estimated with one aptamer to two unit cells (unit cell = four monomers). Verification of the functionality of both aptamers through target binding after S-layer-immobilization on solid supports was proven by laser-induced fluorescence spectroscopy (LIFS), resonant mirror sensor (IAsys), and quartz crystal microbalance with dissipation monitoring (QCM-D), respectively. Hence, this study presents S-layer proteins as an interesting alternative to existing immobilization matrices for recognition biomolecules.

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S-Layer-Based Nanocomposites for Industrial Applications

Raff

Matys

Suhr

et al. 2016

Advances in Experimental Medicine and Biology

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This chapter covers the fundamental aspects of bacterial S-layers: what are S-layers, what is known about them, and what are their main features that makes them so interesting for the production of nanostructures. After a detailed introduction of the paracrystalline protein lattices formed by S-layer systems in nature the chapter explores the engineering of S-layer-based materials. How can S-layers be used to produce "industry-ready" nanoscale bio-composite materials, and which kinds of nanomaterials are possible (e.g., nanoparticle synthesis, nanoparticle immobilization, and multifunctional coatings)? What are the advantages and disadvantages of S-layer-based composite materials? Finally, the chapter highlights the potential of these innovative bacterial biomolecules for future technologies in the fields of metal filtration, catalysis, and bio-functionalization.

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Fluorescence resonance energy transfer by S-layer coupled fluorescence dyes

Cited by 5 publications

References 30 publications

Synthesis of S-Layer Conjugates and Evaluation of Their Modifiability as a Tool for the Functionalization and Patterning of Technical Surfaces

Synthesis of S-Layer Conjugates and Evaluation of Their Modifiability as a Tool for the Functionalization and Patterning of Technical Surfaces

S‐layer proteins as an immobilization matrix for aptamers on different sensor surfaces

S-Layer-Based Nanocomposites for Industrial Applications

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