Kersten S. Rabe

Karlsruhe Institute of Technology

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Christof M. Niemeyer

Karlsruhe Institute of Technology

Theo Peschke

Novartis (Switzerland)

Patrick Bitterwolf

Karlsruhe Institute of Technology

Sabrina Gallus

Karlsruhe Institute of Technology

Ahmed E. Zoheir

National Research Centre

Claude Oelschlaeger

Karlsruhe Institute of Technology

Carmen M. Domínguez

Karlsruhe Institute of Technology

Esther Mittmann

Karlsruhe Institute of Technology

Martin Peng

Karlsruhe Institute of Technology

Norbert Willenbacher

Karlsruhe Institute of Technology

Cooperative Institutions

Karlsruhe Institute of Technology

143

Karlsruhe University of Education

Heidelberg University

TU Dortmund University

Centre National de la Recherche Scientifique

University of Bayreuth

FIZ Karlsruhe – Leibniz Institute for Information Infrastructure

California Institute of Technology

Ludwig-Maximilians-Universität München

FZI Research Center for Information Technology

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Back Cover: A Rationally Designed Connector for Assembly of Protein‐Functionalized DNA Nanostructures (ChemBioChem 12/2016)

ChemBioChem (2016)

Katja J. Koßmann Cornelia Ziegler Alessandro Angelin Rebecca Meyer Marc Skoupi

The back cover picture shows “HOB Art”, an artistic depiction of a DNA origami nanostructure decorated with six HOB proteins. HOB is a halo-based oligonucleotide-binder protein with a rationally engineered binding interface to attain extraordinarily high reaction rates in the covalent ligation with chlorohexyl-modified DNA. More information about the art of HOBbing proteins with DNA can be found in the communication by C. M. Niemeyer et al. on page 1102 in Issue 12, 2016 (DOI: 10.1002/cbic.201600039).

DNA origami

DNA nanotechnology

10.1002/cbic.201600309

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Citations (0)

Biocatalytic Foams from Microdroplet‐Formulated Self‐Assembling Enzymes

Advanced Materials (2023)

Julian Hertel Patrick Bitterwolf Sandra Kröll Astrid Winterhalter Annika J. Weber

Industrial biocatalysis plays an important role in the development of a sustainable economy, as enzymes can be used to synthesize an enormous range of complex molecules under environmentally friendly conditions. To further develop the field, intensive research is being conducted on process technologies for continuous flow biocatalysis in order to immobilize large quantities of enzyme biocatalysts in microstructured flow reactors under conditions that are as gentle as possible in order to realize efficient material conversions. Here, monodisperse foams consisting almost entirely of enzymes covalently linked via SpyCatcher/SpyTag conjugation are reported. The biocatalytic foams are readily available from recombinant enzymes via microfluidic air-in-water droplet formation, can be directly integrated into microreactors, and can be used for biocatalytic conversions after drying. Reactors prepared by this method show surprisingly high stability and biocatalytic activity. The physicochemical characterization of the new materials is described and exemplary applications in biocatalysis are shown using two-enzyme cascades for the stereoselective synthesis of chiral alcohols and the rare sugar tagatose.

Biocatalysis

Microreactor

Environmentally Friendly

Dispersity

10.1002/adma.202303952

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Citations (11)

Solid‐Phase Synthesis and Purification of Protein–DNA Origami Nanostructures

Chemistry - A European Journal (2019)

Teresa Burgahn Ruben Garrecht Kersten S. Rabe Christof M. Niemeyer

Abstract Invited for the cover of this issue are C. M. Niemeyer and co‐workers at the Karlsruhe Institute of Technology (KIT). The cover picture shows a comic hero with magnetic superpowers who pulls pure, protein‐decorated DNA origami nanostructures out of a crude reaction mixture. Read the full text of the article at 10.1002/chem.201805506 .

HERO

10.1002/chem.201900572

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Hybride aus DNA, Proteinen und Kolloiden

Nachrichten aus der Chemie (2011)

Kersten S. Rabe Christof M. Niemeyer

Abstract Neuartige halbsynthetische Hybride entstehen aus Molekülen biologischen und synthetischen Ursprungs. Das Ziel der Forschung sind Funktionseinheiten für Anwendungen in der Sensorik, Katalyse und Materialwissenschaft.

10.1002/nadc.201176781

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Micromechanical Indentation Platform for Rapid Analysis of Viscoelastic Biomolecular Hydrogels

Small Methods (2024)

Phillip Lemke Svenja Moench Paula S. Jäger Claude Oelschlaeger Kersten S. Rabe

Abstract The advent of biomedical applications of soft bioinspired materials has entailed an increasing demand for streamlined and expedient characterization methods meant for both research and quality control objectives. Here, a novel measurement system for the characterization of biological hydrogels with volumes as low as 75 µL was developed. The system is based on an indentation platform equipped with micrometer drive actuators that allow the determination of both the fracture points and Young's moduli of relatively stiff polymers, including agarose, as well as the measurements of viscosity for exceptionally soft and viscous hydrogels, such as DNA hydrogels. The sensitivity of the method allows differentiation between DNA hydrogels produced by rolling circle amplification based on different template sequences and synthesis protocols. In addition, the polymerization kinetics of the hydrogels can be determined by time‐resolved measurements, and the apparent viscosities of even more complex DNA‐based nanocomposites can be measured. The platform presented here thus offers the possibility to characterize a broad variety of soft biomaterials in a targeted, fast, and cost‐effective manner, holding promises for applications in fundamental materials science and ensuring reproducibility in the handling of complex materials.

Characterization

Indentation

Micrometer

Soft materials

Agarose

10.1002/smtd.202400251

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Citations (1)

Orthogonal Protein Decoration of DNA Origami

Angewandte Chemie International Edition (2010)

Barbara Saccà Rebecca Meyer Michael Erkelenz Kathrin Kiko Andreas Arndt

If the face fits: Self-labeling fusion proteins have been used for the site-specific decoration of DNA origami. This method even allows individual faces of the quasi-two-dimensional plane of the nanostructure to be specifically decorated (see picture), thereby enabling directional immobilization and thus control over the accessibility of distinct proteins presented on the structure. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

DNA origami

10.1002/anie.201005931

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Citations (273)

Self-Immobilizing Biocatalysts Maximize Space–Time Yields in Flow Reactors

Catalysts (2019)

Theo Peschke Patrick Bitterwolf Silla Hansen Jannis Gasmi Kersten S. Rabe

Maximizing space–time yields (STY) of biocatalytic flow processes is essential for the establishment of a circular biobased economy. We present a comparative study in which different biocatalytic flow reactor concepts were tested with the same enzyme, the (R)-selective alcohol dehydrogenase from Lactobacillus brevis (LbADH), that was used for stereoselective reduction of 5-nitrononane-2,8-dione. The LbADH contained a genetically encoded streptavidin (STV)-binding peptide to enable self-immobilization on STV-coated surfaces. The purified enzyme was immobilized by physisorption or chemisorption as monolayers on the flow channel walls, on magnetic microbeads in a packed-bed format, or as self-assembled all-enzyme hydrogels. Moreover, a multilayer biofilm with cytosolic-expressed LbADH served as a whole-cell biocatalyst. To enable cross-platform comparison, STY values were determined for the various reactor modules. While mono- and multilayer coatings of the reactor surface led to STY < 10, higher productivity was achieved with packed-bed reactors (STY ≈ 100) and the densely packed hydrogels (STY > 450). The latter modules could be operated for prolonged times (>6 days). Given that our approach should be transferable to other enzymes, we anticipate that compartmentalized microfluidic reaction modules equipped with self-immobilizing biocatalysts would be of great utility for numerous biocatalytic and even chemo-enzymatic cascade reactions under continuous flow conditions.

Biocatalysis

Microreactor

Flow chemistry

Glucose oxidase

10.3390/catal9020164

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Citations (26)

Front Cover: Solid‐Phase Synthesis and Purification of Protein–DNA Origami Nanostructures (Chem. Eur. J. 14/2019)

Chemistry - A European Journal (2019)

Teresa Burgahn Ruben Garrecht Kersten S. Rabe Christof M. Niemeyer

Similar to a comic hero with magnetic superpowers, a microbead assay allows for the efficient extraction of protein-decorated DNA origami nanostructures from crude reaction mixtures. The method provides high yields and delivers pure samples to enable direct AFM analysis for the evaluation of orthogonal immobilization strategies. More information can be found in the Communication by C. M. Niemeyer et al. on page 3483.

Microbead (research)

DNA origami

Front cover

HERO

10.1002/chem.201900571

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The Ternary Complex of Cytochrome f and Cytochrome c: Identification of a Second Binding Site and Competition for Plastocyanin Binding

ChemBioChem (2002)

Peter B. Crowley Kersten S. Rabe Jonathan A. R. Worrall Gerard W. Canters Marcellus Ubbink

The complex of yeast cytochrome c and cytochrome f from the cyanobacterium Phormidium laminosum was investigated by NMR spectroscopy. Chemical shift perturbation analysis reveals that residues around the haem edge of cytochrome c are involved in the complex interface. Binding curves derived from an NMR spectroscopy titration at 10 mM ionic strength indicate that there are two sites for cytochrome c with binding constants of approximately 2 x 10(4) M(-1) and 4 x 10(3) M(-1). A protein docking simulation with NMR-derived constraints identifies two sites, at the front (Site I) and back faces (Site II) of the haem region of cytochrome f. Site I is homologous to the binding site previously determined for the natural cytochrome f partner plastocyanin. Site II may represent the binding site for the Rieske protein in the cytochrome bf complex. Cytochrome c and plastocyanin are shown to compete for binding at Site I. The competition appears to involve electrostatic screening rather than simple steric occlusion of the binding site.

Plastocyanin

Ternary complex

10.1002/1439-7633(20020603)3:6<526::aid-cbic526>3.0.co;2-n

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Citations (37)

High‐Throughput Screening for Terpene‐Synthase‐Cyclization Activity and Directed Evolution of a Terpene Synthase

Angewandte Chemie (2013)

Ryan Lauchli Kersten S. Rabe Karolina Z. Kalbarczyk Amulya Tata Thomas Heel

Ein Substrat für ein colorimetrisches Screening der Cyclisierungsaktivität von Terpensynthasen wurde entwickelt, um das Enzym-Engineering zu erleichtern. Gerichtete Evolution führte zu einer Sesquiterpen-Synthase mit verbesserter Thermostabilität unter Erhaltung der anderen Eigenschaften. Mithilfe der Screening-Methode konnten für eine andere Terpen-Synthase die Expressionsbedingungen und die Stabilisierung im Lysat schnell optimiert werden. PPO=Diphosphat. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.

Terpene

10.1002/ange.201301362

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Citations (11)