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Description [methodology]

We engineer synthetic cellular memory platforms that enable the reconstruction of cellular histories and can be applied as living diagnostics.

A fundamental challenge in biology is to understand how cells function and integrate complex molecular information to perform different behaviors. For example, the differentiation of a stem cell into two daughter cells with distinct identities or the transformation of a normal cell into a cancer cell. This challenge has motivated the creation of numerous technologies facilitating detailed intracellular observations at the level of DNA, RNA, protein, and metabolites. Despite the power of these approaches, they generally require destructive methods and therefore observations are limited to a few snapshots in time or select asynchronous cellular processes. One provocative solution to this is to introduce DNA writing and molecular recording platforms within cells that enable the encoding, storage, and retrieval of molecular information.

Towards the goal of continuously recording molecular events within cells, my laboratory is developing and applying Record-seq, a ‘transcriptional recording’ platform that employs CRISPR spacer acquisition from RNA to capture and convert intracellular RNAs into DNA, permanently storing transcriptional information in the DNA of living cells. The newly acquired sequences serve as transcriptional records, which are retrievable via deep sequencing and can be leverage to reconstruct cellular histories. This technology provides an entirely new mode of interrogating dynamic biological and physiological processes and opens up numerous avenues for future work in engineering cellular systems.

Clinical and immunohistochemical studies indicate that the tumor microenvironment, including stromal and immunocompetent components, plays key roles in the control of tumor progression and response to treatment. Moreover, increased recognition is given to the importance of using human cell- based models to predict the outcome of therapeutic strategies.

The goal of the project is to engineer a 3D human organotypic model of colorectal cancer including associated tumor microenvironment components, as test system for new immune-oncology agents. The further inclusion of hepatocytes in the model in a second phase of the project will enable to investigate, along with the antitumor efficacy, also the possible liver toxicity of the therapeutic agents.

This project focuses on the development of an innovative methodology for the assembly of hierarchical architectures on both solid and polymer platforms. The goal is to design multi-functional systems supporting cascade reactions in 2D networks of nano-compartments (polymersomes, liposomes and combination of thereof) by their controlled anchoring and patterning on surfaces. We will develop strategies and proof-of-principle systems with material turn-over based upon either soft-condensed matter supports (polymers) or hard, metal oxide supports. New soft–hard interfaces will be designed to provide a micro- and nanoscale environment which can modulate properties and activity.

Dimethylfumarate is an emergent pharmaceutical compound with annual sales of 4412 Mio $ in 2016. Currently, the main clinical applications are in treating psoriasis and multiple sclerosis. In addition, dimethylfumarate might be therapeutic against asthma, cancer, inflammatory bowl disease, intracerebral hemorrhage, osteoarthritis, chronic pancreatitis, retinal ischemia, and ischemic stroke.

The goal of this project is to engineer a cell-like device for targeted delivery of the electrophilic drug dimethylfumarate. In the first phase of the project we plan to identify a vesicle based enzyme reaction that is triggered by external stimuli to produce and release dimethylfumarate.

An ideal cell-based diabetes therapy in humans should consist of an autonomous core system enabling closed-loop control of D-glucose sensing and insulin release, coupled to a user-defined control interface that allows the metabolically inert L-glucose to monitor the temporal activity of the therapeutic core. In this context, L-glucose functions as a patient-centred adjuvant molecule that is not only free of hepatic side- effects, but also represents an optimal nutritional sugar for diabetic patients.

The focus of this project is the design and construction of an L-glucose-dependent control interface for future cell-based diabetes therapies and the validation of L-glucose polymersome-dependent control of therapeutic transgene activities in mice.

Our research focuses on the deployment of multiple immobilized molecular catalysts on a flow microreactor platform to convert elementary starting materials over telescoped reactions into chemically and structurally complex products. The interactions of different agents in multiple compartments on a solid-state platform result in a molecular factory.

A combination of multiple catalyst permutations and applied reaction conditions enables screening of diverse parameter spaces for the conversion of suitable starting materials. This approach aims at not only synthesizing one catalysis product from one starting material, but multiple products from the same starting material and whole compound libraries. This bio-inspired approach resembles the biosynthetic processes that are taking place in a biological cell, in which multiple metabolites are often produced from a single molecule.

Our research comprises the design and synthesis of complementary catalysts, linkers and starting materials for heterogeneous catalysis with molecular catalyst monolayers, as well as the immobilization of these catalysts in flow microreactors and conducting synthetic operation on these platforms. This project is in close collaboration with the Mayor group and IBM Research - Zurich in Rüschlikon. The silicon-based flow microreactors are being fabricated by microfabrication techniques, are scalable in the number of compartments, and allow various reaction control features such as nanoscale electrode arrays, catalyst-supporting surfaces, externally controllable micro-heaters and nanophotonic sensing sites to be implemented and to be used as reaction feedback controls.

The chemical and physical processes enabling the transformation of matter in living systems is regulated by complex feedback loops. Such tightly cross-regulated processes enable highly complex reaction cascades as well as transport and exchange mechanisms that have not yet been achieved in synthetic systems. The project „Nanopores as Solid-State Approach to Interlinked Reaction Compartments" strives to simulate isolated feedback mechanisms to investigate the underlying regulation mechanisms in detail and to identify the parameters governing the system.

To fabricate such interlinked reaction compartments, we aim at fabricating nanopore devices based on a solid-state approach using top-down fabrication techniques. Self-assembled monolayers (SAMs) of functional molecular building blocks are physically separated but remain addressable by electrical, optical or electrochemical means. The SAMs are highly oriented which enables correlations between chemical structure and electronic as well as ionic transport properties in single-molecular junctions to be studied. 

Preliminary studies will allow us to mimic a biological response and to investigate isolated feedback mechanisms in detail. Additionally, from a materials point of view, the resulting oligomers may be interesting. Their physical properties are length-dependent and, thanks to a feedback mechanism, their length-distribution may become tunable by specific parameters dictated by the system, leading to a new size-control approach with wide potential applications in material science. Modular systems can easily be expanded with additional functionalities. For example redox-­dependent chromophores that will facilitate the investigation of the systems dynamics as it can be investigated by optical microscopy.

The project is not only geared towards investigating feedback mechanisms across vesicle membranes but also towards integrating vesicles as molecular factories. With such vesicles, molecular devices enabling photo-induced charge separation across the vesicle membrane will be studied. In a later stage of the project, we envisage electrochemical interconnecting of different functionalized vesicles to build up gradients of chemical potentials. 

Molecular systems derive their functional breadth from the interplay of multiple elements. The successful cooperation of these elements is often limited to narrow windows of operation, which are often difficult to identify.

We are optimizing complex in vitro systems so they can successfully operate in these windows. For this, we develop cell free systems that allow the synthesis of multiple catalysts and other protein-based elements, and compartmentalize the synthesis in nanoliter or picoliter-sized droplets. This helps us to investigate thousands of system compositions per minute. We use this to develop design rules for multi-membered systems and prepare such droplets for analysis in a classical way (i.e., by fluorescence) and by label-free methods, such as mass-spectrometry. This way we can optimize system function for a variety of objectives, ranging from enzyme evolution to the engineering of smart systems for metabolic diseases.

Building autonomous synthetic organelles and cells with a defined function using a repertoire of functional modules (toolkit) and containing inside a minimal metabolism for survival, represents the ultimate goal of this project group.

Such complex processors will open a wide variety of possibilities ranging from environmental to medical applications. One of the most important challenges will be to provide a large repertoire of engineered and modular biomolecular-transport and -energy conversion systems for assembly of nanoreactors with diverse functionalities in lipid bilayers and block copolymers.

Initially, modules will include light-­driven proton pumps and proton-driven solute transporters in the membrane, and metabolizing enzymes inside the container. Next, more complex powering systems will be explored such as combinations of light-­driven proton pumps with sodium/proton antiporters with the objective: to energise sodium-driven solute transporters. This will significantly increase the repertoire and specificity of translocating modules.

The availability of numerous, highly specialized membrane proteins in milligram amounts offers the unique opportunity to use them as building blocks and toolkit to assemble molecular factories in the form of nanoreactors and functional surfaces using bottom-up approaches.

This project group has a strong expertise and knowledge in biochemistry, function and structure of membrane proteins. Furthermore, the group already possesses a significant number of recombinant transport proteins for different solutes such as peptides, sugars, amino acids and antibiotics that can be used as modules for engineering and assembly of nanoreactors.

This project shows true interdisciplinary, transversal research: Clinical tests are conducted with light sensitive, molecular systems in partnership with the Friedrich-Miescher Institute of our industry-partner, Novartis. Should the tests be successful, this project could enable blind people to see in black and white again and, eventually, regain their full color vision.

Retinitis pigmentosa (RP) refers to a diverse group of progressive, hereditary diseases of the retina that lead to incurable blindness and affects 2 million people worldwide. Artificial photoreceptors constructed by gene delivery of light-activated channels or pumps (functional molecular modules) to surviving cell types in the remaining retinal circuit have shown to restore photosensitivity in animal models of RP at the level of the retina and cortex as well as behaviourally.

Simply said, in a degenerated macula the first step is missing: there are no more rods and cones that can detect light and subsequently convert light into neural signal. The visual nerves however are intact. In tests with apes and dogs the genetically delivered molecular factories dock successfully with the visual nerve of the eye and are activated by light, producing certain impulses that enables blind animals to see again.

Protein engineering is the field of discovering novel, synthetic proteins or improving a known protein’s activity (e.g., antibody binding affinity for a particular antigen) by using either rational or directed evolution methods. A new method that combines elements of both rational design and directed evolution is deep mutational scanning, which combines high-throughput screening with next-generation DNA sequencing to assess the functional impact of mutations across the protein sequence.

This project aims to establish deep mutational scanning as a viable approach for engineering complex therapeutic proteins. As a starting point, we will use already existing therapeutic monoclonal antibodies against cancer targets, such as Herceptin, Avastin, Cetuximab, and Rituximab, and improve their binding affinity and expression stability. We will also use sequencing data and combine it with biophysical and structural modelling to determine if we can improve the functional scoring systems generated by deep mutational scanning.

One major objective in synthetic biology is the bottom-up assembly of functional nanocells. These structures consist of lipid or polymer membranes, which serve as architectural scaffolds for functional modules such as membrane and soluble proteins. The former is embedded in the membrane, while the latter is encapsulated inside the container. The correct orientation of membrane proteins in the membrane is essential in order to avoid functional short circuits and obtain fully functional nanocells.

In this project, we propose the use of fusion proteins combined with clipping proteins to functionalize nanocells with more than one type of membrane protein.

Scientific and ethical researchers join to identify ethical issues that involve all projects by debating them in an empirically well-informed and argumentatively sound way, and developing sound policy recommendations on how to deal with them.

Molecular Systems Engineering is a rapidly evolving field cutting across traditional disciplinary boundaries. The large extent to which technological aims and design strategies are applied to the biological systems results in an unprecedented level of interference with living nature and the human body.

The risks, benefits, uncertainties as well as novel ideas and paradigms related to this increased potential raise a large set of interesting ethical, societal and policy questions. Moreover, new technological developments resulting from projects involved might impact significantly on the daily lives of future generations and affect their view on the world.

The NCCR Molecular Systems Engineering opens and welcomes an interdisciplinary discussion of exciting and controversial philosophical issues that relate to all of its projects. This can include the meaning of concepts such as “nature”, “life”, “artificiality” or “design” and the relation of these concepts to human design at nanoscale and into the biological world, as well as the design and production of molecular machines and factories, the engineering of cellular functions, the construction of organic-inorganic hybrids and the use of directed evolution as a “designing aid”.

Another area of relevance is future applications with expected benefits and potential risks that may raise ethical and societal issues, e.g. diagnostic or therapeutic tools for medicine or applications towards the production of energy.

A bioethics training module tailored towards the needs of scientists will be developed and offered. Additionally, there are regular interaction and the exchange of experiences with the ethics and public relations office.

This project uses state-of-the-art molecular and genomic editing platforms to engineer immune cells for applications in biotechnology and cellular immunotherapy.

Our ongoing projects are focused on applying molecular and genome editing tools to engineer various types of immune cells. The precise genomic exchange of highly similar immunogenomic genes has not been demonstrated before using genome-editing tools, thus a series of aims and milestones to advance this goal have been established. For example, in one of aims we are engineering mammalian cellular factories for protein production. In another aim we are using precise genome editing to improve cellular therapeutics for transplantation and cancer. We will combine our efforts with the network of NCCR researchers to push the boundaries of immunological systems engineering. 

Scientific Highlights

  • Plug-and-(dis)play mammalian cells. We have used precise genome editing to develop a platform for rapid generation of stable cell lines capable of surface expression and secretion of recombinant proteins. The simplicity of our plug-and-(dis)play platform is highlighted by the fact that it only requires a single transfection and screening step to generate stable cells. We envision these cell lines can be applied for generating recombinant protein reagents and therapeutics. 
  • Reprogramming MHC-specificity immune cells. We have established a proof-of-concept for MHC-allelic replacement, which could be used in the future for improving the donor-host matching, which is a major challenge in allogeneic cellular transplantations in cancer. We used genome editing methods to precisely exchange the MHC region of immune cells, which were then subsequently verified for functions immune activity. Our methods can be applied for the engineering of other immunogenomic regions, which would have value in cellular immunotherapy.

In this project we aim to use visible light to drive electrons across a membrane and to accumulate charges in such a way that NAD+ (nicotinamide adenosine dinucleotide) can be converted to NADH. The latter can then fuel enzymatic cascade reactions which ultimately lead to value-added products that are synthesized in the closed compartment of a molecular factory. The use of vesicles made from block copolymer membranes that make up the closed compartment offers the advantage that the enzymatic chemistry can be performed in a protected environment and that oxidation and reduction products resulting from photochemistry can be spatially separated from one another.

The photophysical and photochemical aspects of this project are addressed by the Wenger group while the enzyme chemistry is taken care of by the Ward group. Vesicles built from block copolymers will be made in collaboration with the groups of Meier and Palivan.

In the first phase of the project, strategies for photodriven electron accumulation are explored in suitable model compounds. For example, covalently linked Ru(bpy)32+ (bpy = 2,2’-bipyridine) – naphthalene diimide (NDI) systems are investigated with a view to reducing NDI to NDI- and finally NDI2- in the course of photoirradiation of the Ru(bpy)32+ photosensitizer in presence of sacrificial or non-sacrificial electron donors. Once the challenge of achieving efficient electron accumulation has been tackled, it will be possible to perform light-driven two-electron reduction of suitable small molecule catalysts which are able to reduce NAD+ to NADH.

In parallel, the Wenger group explores the possibility of obtaining other fuels by means of photochemistry, for example formate from CO2. Formate can act as an electron source for various enzymatic reactions hence this molecule can potentially be used to initiate enzyme cascades. Close interaction between the Wenger and Ward groups is key for this purpose. 

Furthermore, strategies for the oriented incorporation of molecular wires into block copolymer membranes are explored jointly between the Palivan and Wenger groups. In order to obtain net electron transfer from the outside to the inside of the molecular factories made from vesicles, it will be essential to orient donor-bridge-acceptor systems properly in the membrane. 

Possible long-term perspectives include the incorporation of proton pumps into the vesicles in order to transport protons across the membranes, in addition to electrons. This avenue will be explored jointly with the group of Fotiadis. An addition possible avenue is the use of artificial metalloenzymes in the enzyme cascades that rely on engineered anion-π catalysis, as implemented jointly be the groups of Matile and Ward.


M. Adelaide Asnaghi, L. J. Power, A. Barbero, M. Haug, R. Köppl, D. Wendt, I. Martin “Biomarker signatures of quality for engineering nasal chondrocyte-derived cartilage“ Front. Bioeng. Biotechnol. 2020. [DOI]
M. Paraja, X. Hao, S. Matile “Polyether Natural Product Inspired Cascade Cyclizations: Autocatalysis on π-Acidic Aromatic Surfaces“ Angew. Chem. Int. Ed. 2020. [DOI]
X. Guo, Y. Okamoto, M. R. Schreier, T. R. WardO. Wenger “Reductive Amination and Enantioselective Amine Synthesis by Photoredox Catalysis“ Eur. J. Org. Chem. 2020. [DOI]
S. Hirschi, D. Kalbermatter, Z. Ucurum, D. Fotiadis “Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly“ J. Struct. Biol. X 2020. [DOI]
C. E. Meyer, J. Liu, I. Craciun, D. Wu, H. Wang, M. Xie, M. FusseneggerC. G. Palivan “Segregated Nanocompartments Containing Therapeutic Enzymes and Imaging Compounds within DNA-Zipped Polymersome Clusters for Advanced Nanotheranostic Platform“ Small 2020. [DOI]
S. Rigo, M. Kyropoulou, C. Schoenenberger, C. G. Palivan “Battling Bacteria with Free and Surface-Immobilized Polymeric Nanostructures“ Racing for the Surface: Pathogenesis of Implant Infection and Advanced Antimicrobial Strategies 2020. [DOI]
S. Hirschi, D. Fotiadis “Purification of Membrane Proteins by Affinity Chromatography with On-Column Protease Cleavage“ Expression, Purification, and Structural Biology of Membrane Proteins 2020. [DOI]
T. Weinert, V. Panneels “Membrane Protein Preparation for Serial Crystallography Using High-Viscosity Injectors: Rhodopsin as an Example“ Expression, Purification, and Structural Biology of Membrane Proteins 2020. [DOI]
J. López-Andarias, J. Saarbach, D. Moreau, Y. Cheng, E. Derivery, Q. Laurent, M. González-Gaitán, N. Winssinger, N. Sakai, S. Matile “Cell-Penetrating Streptavidin: A General Tool for Bifunctional Delivery with Spatiotemporal Control, Mediated by Transport Systems Such as Adaptive Benzopolysulfane Networks“ J. Am. Chem. Soc. 2020. [DOI]
M. Paraja, S. Matile “Primary Anion–π Catalysis of Epoxide-Opening Ether Cyclization into Rings of Different Sizes: Access to New Reactivity“ Angew. Chem. Int. Ed. 2020. [DOI]
S. Merget, L. Catti, G. Piccini, K. Tiefenbacher “Requirements for Terpene Cyclizations inside the Supramolecular Resorcinarene Capsule: Bound Water and Its Protonation Determine the Catalytic Activity“ J. Am. Chem. Soc. 2020. [DOI]
D. Daubian, J. Gaitzsch, W. Meier “Synthesis and complex self-assembly of amphiphilic block copolymers with a branched hydrophobic poly(2-oxazoline) into multicompartment micelles, pseudo-vesicles and yolk/shell nanoparticles“ Polym. Chem. 2020. [DOI]
B. Zilate, C. Fischer, C. Sparr “Design and application of aminoacridinium organophotoredox catalysts“ Chem. Commun. 2020. [DOI]
D. Haidas, M. Napiorkowska, S. Schmitt, P. Dittrich “Parallel Sampling of Nanoliter Droplet Arrays for Noninvasive Protein Analysis in Discrete Yeast Cultivations by MALDI-MS“ Anal. Chem. 2020. [DOI]
S. Rigo, D. Hürlimann, L. Marot, M. Malmsten, W. MeierC. G. Palivan “Decorating Nanostructured Surfaces with Antimicrobial Peptides to Efficiently Fight Bacteria“ ACS Appl. Bio Mater. 2020. [DOI]
G. Giordano-Attianese, P. Gainza, E. Gray-Gaillard, E. Cribioli, S. Shui, S. Kim, M. Kwak, S. Vollers, A. D. J. Corria Osorio, P. Reichenbach, J. Bonet, B. Oh, M. Irving, G. Coukos, B. Correia “A computationally designed chimeric antigen receptor provides a small-molecule safety switch for T-cell therapy“ Nat. Biotechnol. 2020. [DOI]
K. Krawczyk, L. Scheller, H. Kim, M. Fussenegger “Rewiring of endogenous signaling pathways to genomic targets for therapeutic cell reprogramming“ Nat. Commun. 2020. [DOI]
M. Rybiński, S. Möller, M. Sunnåker, C. Lormeau, J. Stelling “TopoFilter: a MATLAB package for mechanistic model identification in systems biology“ BMC Bioinf. 2020. [DOI]
C. Zelmer, L. P. Zweifel, L. E. Kapinos, I. Craciun, Z. P. Güven, C. G. Palivan, R. Y. H. Lim “Organelle-specific targeting of polymersomes into the cell nucleus“ Proc. Natl. Acad. Sci. U.S.A. 2020. [DOI]
S. Barbato, L. E. Kapinos, C. Rencurel, R. Y. Lim “Karyopherin enrichment at the nuclear pore complex attenuates Ran permeability“ J. Cell Sci. 2020. [DOI]
T. Tanna, F. Schmidt, M. Y. Cherepkova, M. Okoniewski, R. Platt “Recording transcriptional histories using Record-seq“ Nat. Protoc. 2020. [DOI]
T. Einfalt, M. Garni, D. Witzigmann, S. Sieber, N. Baltisberger, J. Huwyler, W. MeierC. G. Palivan “Bioinspired Molecular Factories with Architecture and In Vivo Functionalities as Cell Mimics“ Adv. Sci. 2020. [DOI]
B. M. Gaub, K. C. Kasuba, E. Mace, T. Strittmatter, P. R. Laskowski, S. A. Geissler, A. Hierlemann, M. FusseneggerB. RoskaD. J. Müller “Neurons differentiate magnitude and location of mechanical stimuli“ Proc. Natl. Acad. Sci. U.S.A. 2019. [DOI]
A. Azizoglu, J. Stelling “Controlling cell-to-cell variability with synthetic gene circuits“ Biochem. Soc. Trans. 2019, 47:1795-1804. [DOI]
A. Belluati, V. Mikhalevich, S. Yorulmaz Avsar, D. Daubian, I. Craciun, M. Chami, W. MeierC. G. Palivan “How do the properties of amphiphilic polymer membranes influence the functional insertion of peptide pores?“ Biomacromolecules 2019. [DOI]
A. Mazé, Y. Benenson “Artificial signaling in mammalian cells enabled by prokaryotic two-component system“ Nat. Chem. Biol. 2019. [DOI]
M. Kyropoulou, S. DiLeone, A. Lanzilotto, E. C. Constable, C. E. HousecroftW. MeierC. G. Palivan “Porphyrin Containing Polymersomes with Enhanced ROS Generation Efficiency: In Vitro Evaluation“ Macromol. Biosci. 2019. [DOI]
P. Gainza, F. Sverrisson, F. Monti, E. Rodolà, D. Boscaini, M. M. Bronstein, B. Correia “Deciphering interaction fingerprints from protein molecular surfaces using geometric deep learning“ Nat. Methods 2019. [DOI]
L. Oberhauser, S. Granziera, A. Colom, A. Goujon, V. Lavallard, S. Matile, A. Roux, T. Brun, P. Maechler “Palmitate and oleate modify membrane fluidity and kinase activities of INS-1E β-cells alongside altered metabolism-secretion coupling“ Biochim. Biophys. Acta, Mol. Cell Res. 2019. [DOI]
V. C. Fäseke, F. C. Raps, C. Sparr “Polyketide Cyclizations for the Synthesis of Polyaromatics“ Angew. Chem. Int. Ed. 2019. [DOI]
T. Brandl, C. Kerzig, L. Le Pleux, A. Prescimone, O. WengerM. Mayor “Improved Photostability of a Cu(I) Complex by Macrocyclization of the Phenanthroline Ligands“ Chem. Eur. J. 2019. [DOI]
N. Jain, T. Shahal, T. Gabrieli, N. Gilat, D. Torchinsky, Y. Michaeli, V. Vogel, Y. Ebenstein “Global modulation in DNA epigenetics during pro-inflammatory macrophage activation“ Epigenetics 2019, 14:1183-1193. [DOI]
D. Wu, S. Rigo, S. Di Leone, A. Belluati, E. C. Constable, C. E. HousecroftC. G. Palivan “Brushing the surface: cascade reactions between immobilized nanoreactors“ Nanoscale 2019. [DOI]
C. Fischer, C. Kerzig, B. Zilate, O. WengerC. Sparr “Modulation of Acridinium Organophotoredox Catalysts Guided by Photophysical Studies“ ACS Catal. 2019. [DOI]
T. Pesch, L. Bonati, W. Kelton, C. Parola, R. A. Ehling, L. Csepregi, D. Kitamura, S. Reddy “Molecular Design, Optimization, and Genomic Integration of Chimeric B Cell Receptors in Murine B Cells“ Front. Immunol. 2019. [DOI]
M. della Volpe-Waizel, H. C. Zuche, U. Müller, A. Rickmann, H. Scholl, M. G. Todorova “Metabolic monitoring of transcorneal electrical stimulation in retinitis pigmentosa“ Graefes Arch. Clin. Exp .Ophthalmol. 2019. [DOI]
X. Zhang, N. Sakai, S. Matile “Methyl Scanning for Mechanochemical Chalcogen-Bonding Cascade Switches“ ChemistryOpen 2019. [DOI]
S. Wu, Y. Zhou, D. Gerngross, M. Jeschek, T. R. Ward “Chemo-enzymatic cascades to produce cycloalkenes from bio-based resources“ Nat. Commun. 2019. [DOI]
A. Castrogiovanni, P. Herr, X. Guo, C. Larsen, C. SparrO. Wenger “Shortcuts for Electron-Transfer through the Secondary Structure of Helical Oligo-1,2-naphthylenes“ Chem. Eur. J. 2019. [DOI]
K. Strakova, A. I. Poblador-Bahamonde, N. Sakai, S. Matile “Fluorescent Flipper Probes: Comprehensive Twist Coverage“ Chem. Eur. J. 2019. [DOI]
R. M. Witzig, C. Sparr “Synthesis of Enantioenriched Tetra-ortho-3,3′-substituted Biaryls by Small-Molecule-Catalyzed Noncanonical Polyketide Cyclizations“ Synlett 2019. [DOI]
J. Folini, C. Huang, J. C. Anderson, W. Meier, J. Gaitzsch “Novel monomers in radical ring-opening polymerisation for biodegradable and pH responsive nanoparticles“ Polym. Chem. 2019. [DOI]
R. Schubert, S. Herzog, S. Trenholm, B. RoskaD. J. Müller “Magnetically guided virus stamping for the targeted infection of single cells or groups of cells“ Nat. Protoc. 2019. [DOI]
Q. Laurent, M. Berthet, Y. Cheng, N. Sakai, S. Barluenga, N. Winssinger, S. Matile “Probing for Thiol-Mediated Uptake into Bacteria“ ChemBioChem 2019. [DOI]
D. Bojar, M. Fussenegger “The Role of Protein Engineering in Biomedical Applications of Mammalian Synthetic Biology“ Small 2019. [DOI]
V. Chimisso, C. Fodor, W. Meier “Effect of Divalent Cation on Swelling Behavior of Anionic Microgels: Quantification and Dynamics of Ion Uptake and Release“ Langmuir 2019. [DOI]
R. M. Witzig, V. C. Fäseke, D. Häussinger, C. Sparr “Atroposelective synthesis of tetra-ortho-substituted biaryls by catalyst-controlled non-canonical polyketide cyclizations“ Nat. Catal. 2019. [DOI]
J. G. Camp, R. Platt, B. Treutlein “Mapping human cell phenotypes to genotypes with single-cell genomics“ 2019. [DOI]
A. Bornhof, M. Vázquez-Nakagawa, L. Rodríguez-Pérez, M. Ángeles Herranz, N. Sakai, N. Martín, S. Matile, J. López-Andarias “Anion–π Catalysis on Carbon Nanotubes“ Angew. Chem. Int. Ed. 2019. [DOI]
V. Chimisso, V. Maffeis, D. Hürlimann, C. G. PalivanW. Meier “Self-Assembled Polymeric Membranes and Nanoassemblies on Surfaces: Preparation, Characterization, and Current Applications“ Macromol. Biosci. 2019. [DOI]
M. Macchione, A. Goujon, K. Strakova, H. V. Humeniuk, G. Licari, E. Tajkhorshid, N. Sakai, S. Matile “A Chalcogen-Bonding Cascade Switch for Planarizable Push–Pull Probes“ Angew. Chem. Int. Ed. 2019. [DOI]
M. Baghernejad, C. Van Dyck, J. Bergfield, D. R. Levine, A. Gubicza, J. D. Tovar, M. Calame, P. Broekmann, W. Hong “Quantum interference enhanced chemical responsivity in single-molecule dithienoborepin junctions“ Chem. Eur. J. 2019. [DOI]
D. Kaldre, F. Gallou, C. Sparr, M. Parmentier “Interface-rich Aqueous Systems for Sustainable Chemical Synthesis“ Chimia 2019, 73:714-19. [DOI]
S. Wu, Y. Zhou, J. G. Rebelein, M. Kuhn, H. Mallin, J. Zhao, N. V. Igareta, T. R. Ward “Breaking Symmetry: Engineering Single-Chain Dimeric Streptavidin as Host for Artificial Metalloenzymes“ J. Am. Chem. Soc. 2019. [DOI]
V. Sabatino, J. G. Rebelein, T. R. Ward ““Close-to-Release”: Spontaneous Bioorthogonal Uncaging Resulting from Ring-Closing Metathesis“ J. Am. Chem. Soc. 2019. [DOI]
P. Jusková, Y. R. F. Schmid, A. Stucki, S. Schmitt, M. Held, P. Dittrich ““Basicles”: Microbial Growth and Production Monitoring in Giant Lipid Vesicles“ ACS Appl. Mater. Interfaces 2019. [DOI]
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L. Catti, A. Pöthig, K. Tiefenbacher “Host-Catalyzed Cyclodehydration–Rearrangement Cascade Reaction of Unsaturated Tertiary Alcohols“ Adv. Synth. Catal. 2017, 359:1331-38. [DOI]
A. Lanzilotto, M. Kuss-Petermann, O. Wenger, E. C. Constable, C. E. Housecroft “Homoleptic complexes of a porphyrinatozinc(ii)-2,2':6',2''-terpyridine ligand“ Photochem. Photobiol. Sci. 2017, 16:585-95. [DOI]
R. Platt, Y. Zhou, I. M. Slaymaker, A. S. Shetty, N. R. Weisbach, J. Kim, J. Sharma, M. Desai, S. Sood, H. R. Kempton, G. R. Crabtree, G. Feng, F. Zhang “Chd8 Mutation Leads to Autistic-like Behaviors and Impaired Striatal Circuits“ Cell Rep. 2017, 19:335-50. [DOI]
Y. F. Dufrene, T. Ando, R. Garcia, D. Alsteens, D. Martinez-Martin, A. Engel, C. Gerber, D. J. Muller, D. J. Müller “Imaging modes of atomic force microscopy for application in molecular and cell biology“ Nat. Nanotechnol. 2017, 12(4):295-307. [DOI]
S. Reddy “Reprogramming MHC specificity by CRISPR-Cas9-assisted cassette exchange“ Sci. Rep. 2017, 7:45775. [DOI]
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M. Kuss-Petermann, M. Orazietti, M. Neuburger, P. Hamm, O. Wenger “Intramolecular Light-Driven Accumulation of Reduction Equivalents by Proton-Coupled Electron Transfer“ J. Am. Chem. Soc. 2017. [DOI]
G. Gunkel-Grabole, C. G. PalivanW. Meier “Nanostructured Surfaces through Immobilization of Self-Assembled Polymer Architectures Using Thiol–Ene Chemistry“ Macromol. Mater. Eng. 2017, 302:1600363. [DOI]
M. Garni, S. Thamboo, C. Schoenenberger, C. G. Palivan “Biopores/membrane proteins in synthetic polymer membranes“ Biochim. Biophys. Acta, Biomembr. 2017, 1859:619-38. [DOI]
Y. M. Klein, A. Lanzilotto, A. Prescimone, K. W. Krämer, S. Decurtins, S. Liu, E. C. Constable, C. E. Housecroft “Coordination behaviour of 1-(3,2':6',3''-terpyridin-4'-yl)ferrocene: structure and magnetic and electrochemical properties of a tetracopper dimetallomacrocycle“ Polyhedron 2017, 129:71-76. [DOI]
I. Craciun, G. Gunkel-Grabole, A. Belluati, C. G. PalivanW. Meier “Expanding the potential of MRI contrast agents through multifunctional polymeric nanocarriers“ Nanomedicine 2017, 12:811-17. [DOI]
D. Alsteens, H. E. Gaub, R. Newton, M. Pfreundschuh, C. Gerber, D. J. Müller “Atomic force microscopy-based characterization and design of biointerfaces“ Nat. Rev. Mater. 2017, 2(5):17008. [DOI]
B. M. Gaub, D. J. Müller “Mechanical Stimulation of Piezo1 Receptors Depends on Extracellular Matrix Proteins and Directionality of Force“ Nano Lett. 2017, 17(3):2064-72
M. Skaisgirski, X. Guo, O. Wenger “Electron Accumulation on Naphthalene Diimide Photosensitized by [Ru(2,2′-Bipyridine)3]2+“ Inorg. Chem. 2017, 56:2432-39. [DOI]
S. MatileW. MeierC. G. Palivan “Strain-Promoted Thiol-Mediated Cellular Uptake of Giant Substrates: Liposomes and Polymersomes“ Angew. Chem. Int. Ed. 2017, 56:2947-50. [DOI]
D. J. Müller, H. E. Gaub “Membrane proteins scrambling through a folding landscape“ Science 2017. [DOI]
N. Zhang, V. Milleret, G. Thompson-Steckel, N. Huang, J. Vörös, B. R. Simona, M. Ehrbar “Soft Hydrogels Featuring In-Depth Surface Density Gradients for the Simple Establishment of 3D Tissue Models for Screening Applications“ SLAS Discov. 2017, 22:635-44. [DOI]
S. Lörcher, W. Meier “Cosolvent fractionation of PMOXA-b-PDMS-b-PMOXA: Bulk separation of triblocks from multiblocks“ Eur. Polym. J. 2017. [DOI]
E. V. Konishcheva, U. E. Zhumaev, W. Meier “PEO-b-PCL-b-PMOXA Triblock Copolymers: From Synthesis to Microscale Polymersomes with Asymmetric Membrane“ Macromolecules 2017. [DOI]
P. Baumann, M. Spulber, O. Fischer, A. Car, W. Meier “Investigation of Horseradish Peroxidase Kinetics in an “Organelle-Like” Environment“ Small 2017, 13:1603943. [DOI] [More Information]
P. Morelli, S. Matile “Sidechain Engineering in Cell-Penetrating Poly(disulfide)s“ Helv. Chim. Acta 2017, 100. [DOI]
P. Mohammadi, N. Beerenwinkel, Y. Benenson “Automated Design of Synthetic Cell Classifier Circuits Using a Two-Step Optimization Strategy“ 2017. [DOI]
D. Gregorowius, N. Biller‐Andorno, A. Deplazes Zemp, N. Biller-Andorno “The role of scientific self‐regulation for the control of genome editing in the human germline“ EMBO Rep. 2017, 18:355-58. [DOI]
M. Macchione, N. Chuard, N. Sakai, S. Matile “Planarizable Push–Pull Probes: Overtwisted Flipper Mechanophores“ ChemPlusChem 2017. [DOI]
R. Wehlauch, S. M. Grendelmeier, H. Miyatake-Ondozabal, A. H. Sandtorv, M. Scherer, K. Gademann “Investigating Biogenetic Hypotheses of the Securinega Alkaloids: Enantioselective Total Syntheses of Secu’amamine E/ent-Virosine A and Bubbialine“ Org. Lett. 2017, 19:548-51. [DOI]
Q. Zhang, L. Catti, V. R. I. Kaila, K. Tiefenbacher “To catalyze or not to catalyze: elucidation of the subtle differences between the hexameric capsules of pyrogallolarene and resorcinarene“ Chem. Sci. 2017. [DOI]
M. Bharadwaj, N. Strohmeyer, G. P. Colo, J. Helenius, N. Beerenwinkel, H. B. Schiller, R. Fässler, D. J. Müller “αV-class integrins exert dual roles on α5β1 integrins to strengthen adhesion to fibronectin“ Nat. Commun. 2017. [DOI]
Q. Verolet, M. Dal Molin, A. Colom, A. Roux, L. Guénée, N. Sakai, S. Matile “Twisted Push‐Pull Probes with Turn‐On Sulfide Donors“ Helv. Chim. Acta 2017, 100:e1600328. [DOI]
A. Pannwitz, A. Prescimone, O. Wenger “Ruthenium(II)–Pyridylimidazole Complexes as Photoreductants and PCET Reagents“ Eur. J. Inorg. Chem. 2017, 2017:609-15. [DOI]
L. A. Büldt, X. Guo, R. Vogel, A. Prescimone, O. Wenger “A Tris (diisocyanide) chromium (0) Complex Is a Luminescent Analog of Fe (2, 2′-Bipyridine) 32+“ J. Am. Chem. Soc. 2017, 139:985-92. [DOI]
M. Muller, D. Auslander, A. Spinnler, J. Sikorski, M. Folcher, M. Fussenegger “Designed cell consortia as fragrance-programmable analog-to-digital converters“ 2017, 13:309-16. [DOI]
R. L. Stoop, K. Thodkar, M. Sessolo, H. J. Bolink, C. Schönenberger, M. Calame “Charge Noise in Organic Electrochemical Transistors“ Phys. Rev. Appl. 2017, 7:014009. [DOI]
S. Schuerle, I. A. Vizcarra, J. Moeller, M. S. Sakar, B. Özkale, A. M. Lindo, F. Mushtaq, I. Schoen, S. Pané, V. Vogel, B. J. Nelson “Robotically controlled microprey to resolve initial attack modes preceding phagocytosis“ Sci. Rob. 2017, 2:eaah6094. [DOI]
M. Jeschek, M. O. Bahls, V. Schneider, P. Marlière, T. R. WardS. Panke “Biotin-independent Strains of Escherichia coli for Enhanced Streptavidin Production“ Metab. Eng. 2017, 40:33-40. [DOI]
M. Kuss-Petermann, O. Wenger “Pump-Pump-Probe Spectroscopy of a Molecular Triad Monitoring Detrimental Processes for Photoinduced Charge Accumulation“ Helv. Chim. Acta 2017, 100:e1600283. [DOI]
J. Schreiber, M. Arter, N. Lapique, B. Haefliger, Y. Benenson “Model‐guided combinatorial optimization of complex synthetic gene networks“ Mol. Syst. Biol. 2016, 12:899. [DOI]
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S. Soleimanpour, A. Colom, E. Derivery, M. Gonzalez-Gaitan, A. Roux, N. Sakai, S. Matile “Headgroup engineering in mechanosensitive membrane probes“ Chem. Commun. 2016, 52:14450-53. [DOI]
M. Xie, H. Ye, H. Wang, G. Charpin-El Hamri, C. Lormeau, P. Saxena, J. StellingM. Fussenegger “β-cell–mimetic designer cells provide closed-loop glycemic control“ Science 2016, 354:1296-1301. [DOI]
D. Gregorowius, A. Deplazes-Zemp “Societal impact of synthetic biology: responsible research and innovation (RRI)“ Essays Biochem. 2016, 60:371-79. [DOI]
C. Wang, F. N. Miros, J. Mareda, N. Sakai, S. Matile “Asymmetric Anion–π Catalysis on Perylenediimides“ Angew. Chem. Int. Ed. 2016, 55:14422-26. [DOI]
Y. M. Klein, A. Prescimone, E. C. Constable, C. E. Housecroft “Coordination Behaviour of 1-(4, 2′: 6′, 4 ″-terpyridin-4′-yl) ferrocene and 1-(3, 2′: 6′, 3 ″-terpyridin-4′-yl) ferrocene: Predictable and Unpredictable Assembly Algorithms“ Aust. J. Chem. 2016, 70:468. [DOI]
L. O. Herrmann, A. Olziersky, C. Gruber, G. Puebla-Hellmann, U. Drechsler, T. von Arx, K. Venkatesan, L. Novotny, E. Lörtscher “Fabrication of NEMS actuated plasmonic antenna platform for the study of optical forces and field enhancements in hot-spots“ Asia Communications and Photonics Conference 2016 2016:AS4B.2. [DOI]
T. Serdiuk, D. Balasubramaniam, J. Sugihara, S. A. Mari, H. R. Kaback, D. J. Müller “YidC assists the stepwise and stochastic folding of membrane proteins“ Nat. Chem. Biol. 2016, 12:911-17. [DOI]
D. Alsteens, R. Newton, R. Schubert, D. Martinez-Martin, M. Delguste, B. RoskaD. J. Müller “Nanomechanical mapping of first binding steps of a virus to animal cells“ Nat. Nanotechnol. 2016:DOI:10.1038/nnano.2016.228. [DOI]
R. Gnügge, L. Dharmarajan, M. Lang, J. Stelling “An Orthogonal Permease–Inducer–Repressor Feedback Loop Shows Bistability“ ACS Synth. Biol. 2016, 5:1098-107. [DOI]
J. Liu, V. Postupalenko, S. Lörcher, D. Wu, M. Chami, W. MeierC. G. Palivan “DNA-Mediated Self-Organization of Polymeric Nanocompartments Leads to Interconnected Artificial Organelles“ Nano Lett. 2016:DOI: 10.1021/acs.nanolett.6b03430. [DOI] [More Information]
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R. Kojima, D. Aubel, M. Fussenegger “Toward a world of theranostic medication: Programming biological sentinel systems for therapeutic intervention“ Adv. Drug Delivery Rev. 2016, 105:66-76. [DOI]
Z. Liu, V. Lebrun, T. Kitanosono, H. Mallin, V. Köhler, D. Häussinger, D. Hilvert, S. Kobayashi, T. R. Ward “Upregulation of an Artificial Zymogen by Proteolysis“ Angew. Chem. Int. Ed. 2016, 55:11587-90. [DOI]
N. Chuard, K. Fujisawa, P. Morelli, J. Saarbach, N. Winssinger, P. Metrangolo, G. Resnati, N. Sakai, S. Matile “Activation of Cell-Penetrating Peptides with Ionpair−π Interactions and Fluorophiles“ J. Am. Chem. Soc. 2016, 138:11264-71. [DOI]
L. A. Büldt, X. Guo, A. Prescimone, O. Wenger “A Molybdenum (0) Isocyanide Analogue of Ru (2, 2′‐Bipyridine) 32+: A Strong Reductant for Photoredox Catalysis“ Angew. Chem. Int. Ed. 2016, 55:11247-50. [DOI]
M. Jeschek, R. Reuter, T. Heinisch, C. Trindler, J. Klehr, S. PankeT. R. Ward “Directed evolution of artificial metalloenzymes for in vivo metathesis“ Nature 2016, doi:10.1038/nature19114. [DOI] [More Information]
M. Pogson, C. Parola, W. J. Kelton, P. Heuberger, S. Reddy “Immunogenomic engineering of a plug-and-(dis)play hybridoma platform“ Nat. Commun. 2016, 7:12535. [DOI]
M. Hestericová, M. R. Correro, M. Lenz, P. F. Corvini, P. Shahgaldian, T. R. Ward “Immobilization of an artificial imine reductase within silica nanoparticles improves its performance“ Chem. Commun. 2016, 52:9462-65. [DOI]
S. J. Sigg, F. Santini, A. Najer, P. U. Richard, W. MeierC. G. Palivan “Nanoparticle-based highly sensitive MRI contrast agents with enhanced relaxivity in reductive milieu“ Chem. Commun. 2016, 52:9937-40. [DOI]
Z. P. Guven, B. Ustbas, K. M. Harkness, H. Coskun, C. P. Joshi, T. M. D. Besong, F. Stellacci, O. M. Bakr, O. Akbulut “Synthesis and characterization of mixed ligand chiral nanoclusters“ Dalton Trans. 2016, 45:11297-300. [DOI]
S. Benz, M. Macchione, Q. Verolet, J. Mareda, N. Sakai, S. Matile “Anion Transport with Chalcogen Bonds“ J. Am. Chem. Soc. 2016, 138:9093-96. [DOI]
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D. Harder, S. Hirschi, Z. Ucurum, R. Goers, W. MeierD. J. MüllerD. Fotiadis “Engineering a Chemical Switch into the Light-driven Proton Pump Proteorhodopsin by Cysteine Mutagenesis and Thiol Modification“ Angew. Chem. Int. Ed.  2016, 55:8846. [DOI]
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Y. OkamotoT. R. WardO. Wenger “From Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories“ Chimia 2016, 6:395. [DOI]
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C. E. HousecroftC. G. Palivan, K. Gademann, W. Meier, M. Calame, V. Mikhalevich, X. Zhang, E. Piel, M. Szponarski, A. Wiesler, A. Lanzilotto, E. C. Constable, A. Fanget, R. Stoop “‘Active surfaces’ as Possible Functional Systems in Detection and Chemical (Bio) Reactivity“ Chimia 2016, 6:402. [DOI]
G. Puebla-Hellmann, M. MayorE. Lörtscher “Functional Nanopores: A Solid-state Concept for Artificial Reaction Compartments and Molecular Factories“ Chimia 2016, 6:432. [DOI]
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M. Garni, T. Einfalt, M. Lomora, A. Car, W. MeierC. G. Palivan “Artificial Organelles: Reactions inside Protein–Polymer Supramolecular Assemblies“ Chimia 2016, 6:424. [DOI]
S. Vujica, C. Zelmer, R. Panatala, R. Y. H. Lim “Nucleocytoplasmic Transport: A Paradigm for Molecular Logistics in Artificial Systems“ Chimia 2016, 6:413. [DOI]
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R. Heidari, B. Elger, R. Stutzki “On the Brink of Shifting Paradigms, Molecular Systems Engineering Ethics Needs to Take a Proactive Approach“ Chimia 2016, 6:449. [DOI]
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T. M. Roberts, F. Rudolf, A. Meyer, R. Pellaux, E. Whitehead, S. Panke, M. Held “Identification and Characterisation of a pH-stable GFP“ Sci. Rep. 2016, 6:28166. [DOI]
A. Bolag, N. Sakai, S. Matile “Dipolar Photosystems: Engineering Oriented Push–Pull Components into Double- and Triple-Channel Surface Architectures“ Chem. Eur. J. 2016, 22:9006-14. [DOI]
M. JeschekS. PankeT. R. Ward “Chapter Twenty-Three-Periplasmic Screening for Artificial Metalloenzymes“ Methods Enzymol. 2016, 580:539-56. [DOI]
R. Boggavarapu, S. Hirschi, D. Harder, M. Meury, Z. Ucurum, M. J. Bergeron, D. Fotiadis “Purification of Human and Mammalian Membrane Proteins Expressed in Xenopus laevis Frog Oocytes for Structural Studies“ Heterologous Expression of Membrane Proteins 2016, 1432:223-42. [DOI]
J. Foolen, J. Shiu, M. Mitsi, Y. Zhang, C. S. Chen, V. Vogel “Full-Length Fibronectin Drives Fibroblast Accumulation at the Surface of Collagen Microtissues during Cell-Induced Tissue Morphogenesis“ PLoS One 2016, 11:e0160369. [DOI]
Y. M. Klein, A. Prescimone, M. B. Pitak, S. J. Coles, E. C. Constable, C. E. Housecroft “Constructing chiral MOFs by functionalizing 4, 2′: 6′, 4′′-terpyridine with long-chain alkoxy domains: rare examples of neb nets“ CrystEngComm 2016, 18:4704-07. [DOI]
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E. A. Miłopolska, M. Kuss-Petermann, M. Neuburger, O. WengerT. R. Ward “N-Heterocyclic carbene ligands bearing a naphthoquinone appendage: Synthesis and coordination chemistry“ Polyhedron 2016, 103:261-66. [DOI]
P. Morelli, X. Martin-Benlloch, R. Tessier, J. Waser, N. Sakai, S. Matile “Ethynyl benziodoxolones: functional terminators for cell-penetrating poly(disulfide)s“ Polym. Chem. 2016, 7:3465-70. [DOI]
M. Pogson, W. Kelton, S. Reddy “Microscale Technologies for High-Throughput Analysis of Immune Cells“ Microscale Technologies for Cell Engineering 2016:219-30. [DOI]
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M. Wipf, R. L. Stoop, G. Navarra, S. Rabbani, B. Ernst, K. Bedner, C. Schönenberger, M. Calame “Label-Free FimH Protein Interaction Analysis Using Silicon Nanoribbon BioFETs“ ACS Sens. 2016:DOI: 10.1021/acssensors.6b00089. [DOI]
T. Raschle, P. Rios Flores, C. Opitz, D. J. Müller, S. Hiller “Monitoring Backbone Hydrogen-Bond Formation in β-Barrel Membrane Protein Folding“ Angew. Chem. Int. Ed. 2016, 55:5952-55. [DOI]
R. L. Stoop, M. Wipf, S. Müller, K. Bedner, I. A. Wright, C. J. Martin, E. C. Constable, A. Fanget, C. Schönenberger, M. Calame “Implementing Silicon Nanoribbon Field-Effect Transistors as Arrays for Multiple Ion Detection“ Biosensors 2016, 6:21. [DOI]
Y. Sakiyama, A. Mazur, L. E. Kapinos, R. Y. H. Lim “Spatiotemporal dynamics of the nuclear pore complex transport barrier resolved by high-speed atomic force microscopy“ Nat. Nanotechnol. 2016:DOI: 10.1038/nnano.2016.62. [DOI]
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Y. Okamoto, V. Köhler, C. E. Paul, F. Hollmann, T. R. Ward “Efficient In Situ Regeneration of NADH Mimics by an Artificial Metalloenzyme“ ACS Catal. 2016, 6:3553. [DOI]
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Y. Okamoto, V. Köhler, T. R. Ward “An NAD(P)H-Dependent Artificial Transfer Hydrogenase for Multienzymatic Cascades“ J. Am. Chem. Soc. 2016, 138:5781. [DOI]
S. Lascano, K. Zhang, R. Wehlauch, K. Gademann, N. Sakaiab, S. Matile “The third orthogonal dynamic covalent bond“ Chem. Sci. 2016, 7:4720. [DOI]
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J. Krol, B. Roska “Rods Feed Cones to Keep them Alive“ Cell 2015, 161:706-08. [DOI]
T. Kim, M. Folcher, G. Charpin-El Hamri, M. Fussenegger “A synthetic cGMP-sensitive gene switch providing Viagra((R))-controlled gene expression in mammalian cells and mice“ Metab. Eng. 2015, 29:169-79. [DOI]
J. Lopez-Andarias, A. Bolag, C. Nancoz, E. Vauthey, C. Atienza, N. Sakai, N. Martin, S. Matile “Electron-deficient fullerenes in triple-channel photosystems“ Chem. Commun. 2015, 51:7543-45. [DOI]
N. Hostettler, I. A. Wright, B. Bozic-Weber, E. C. Constable, C. E. Housecroft “Dye-sensitized solar cells with hole-stabilizing surfaces: “inorganic” versus “organic” strategies“ RSC Adv. 2015, 5:37906. [DOI]
A. Deplazes Zemp, D. Gregorowius, N. Biller-Andorno “Different Understandings of Life as an Opportunity to Enrich the Debate About Synthetic Biology“ Springer, Nanoethics 2015, 9:179. [DOI]
A. Hochstetter, E. Stellamanns, S. Deshpande, S. Uppaluri, M. Engstler, T. Pfohl “Microfluidics-based single cell analysis reveals drug-dependent motility changes in trypanosomes“ Lab Chip 2015, 15:1961-68. [DOI]
F. M. Heydenreich, Z. Vuckovic, M. Matkovic, D. B. Veprintsev “Stabilization of G protein-coupled receptors by point mutations“ Front. Pharmacol. 2015, 6:82. [DOI] [More Information]
G. Emilsson, R. L. Schoch, L. Feuz, F. Hook, R. Y. Lim, A. B. Dahlin “Strongly stretched protein resistant poly(ethylene glycol) brushes prepared by grafting-to“ ACS Appl. Mater. Interfaces 2015, 7:7505-15. [DOI]
M. Dal Molin, Q. Verolet, S. Soleimanpour, S. Matile “Mechanosensitive membrane probes“ Chem. Eur. J. 2015, 21:6012-21. [DOI]
Y. Zhao, G. Huang, C. Besnard, J. Mareda, N. Sakai, S. Matile “Big, Strong, Neutral, Twisted, and Chiral π Acids“ Chem. Eur. J. 2015, 21:6202-07. [DOI]
J. Kowal, D. Wu, V. MikhalevichC. G. PalivanW. Meier “Hybrid Polymer–Lipid Films as Platforms for Directed Membrane Protein Insertion“ Langmuir 2015, 31:4868. [DOI]
T. Serdiuk, J. Sugihara, S. Mari, H. . Kaback, D. J. Müller “Observing a Lipid-Dependent Alteration in Single Lactose Permeases“ Structure 2015, 23:754-61. [DOI]
D. Milić, D. B. Veprintsev “Large-scale production and protein engineering of G protein-coupled receptors for structural studies“ Front. Pharmacol. 2015, 6:66. [DOI] [More Information]
M. Lomora, M. Garni, F. Itel, P. Tanner, M. Spulber, C. G. Palivan “Polymersomes with engineered ion selective permeability as stimuli-responsive nanocompartments with preserved architecture“ Biomaterials 2015, 53:406. [DOI]
M. Mehling, T. Frank, C. Albayrak, S. Tay “Real-time tracking, retrieval and gene expression analysis of migrating human T cells“ Lab Chip 2015, 15:1217. [DOI]
K. Gademann “Copy, Edit, and Paste: Natural Product Approaches to Biomaterials and Neuroengineering“ Acc. Chem. Res. 2015, 48:731. [DOI]
M. Lomora, I. A. Dinu, C. G. Palivan “Selective ion-permeable membranes by insertion of biopores into polymersomes“ Phys. Chem. 2015, 17:15538. [DOI]
R. S. Wagner, L. E. Kapinos, N. J. Marshall, M. Stewart, R. Y. Lim “Promiscuous binding of Karyopherinbeta1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics“ Biophys. J. 2015, 108:918-27. [DOI]
J. M. Nunes, M. Mayer-Hartl, F. U. Hartl, D. J. Müller “Action of the Hsp70 chaperone system observed with single proteins“ Nat. Commun. 2015, 6:6307. [DOI] [More Information]
H. Miyatake-Ondozabal, E. Kaufmann, K. Gademann “Total Synthesis of the Protected Aglycon of Fidaxomicin (Tiacumicin B, Lipiarmycin A3)“ Angew. Chem. Int. Ed. 2015, 54:1933. [DOI]
B. Geering, M. Fussenegger “Synthetic immunology: modulating the human immune system“ Trends Biotechnol. 2015, 33:65-79. [DOI]
R. A. Kellogg, S. Tay “Noise facilitates transcriptional control under dynamic inputs“ Cell 2015, 160:381-92. [DOI]
M. Spulber, P. Baumann, J. Liu, C. G. Palivan “Ceria loaded nanoreactors: a nontoxic superantioxidant system with high stability and efficacy“ Nanoscale 2015, 7:1411. [DOI]
P. D. Bosshart, A. Engel, D. Fotiadis “High-Resolution Atomic Force Microscopy Imaging of Rhodopsin in Rod Outer Segment Disk Membranes“ Rhodopsin 2015:189-203. [DOI]
B. Dielacher, R. F. Tiefenauer, J. Junesch, J. Vörös “Iodide sensing via electrochemical etching of ultrathin gold films“ Nanotechnology 2015, 26:025202. [DOI]
T. Quinto, D. Haussinger, V. Kohler, T. R. Ward “Artificial metalloenzymes for the diastereoselective reduction of NAD(+) to NAD(2)H“ Org. Biomol. Chem. 2015, 13:357-60. [DOI]
N. Chuard, G. Gasparini, A. Roux, N. Sakai, S. Matile “Cell-penetrating poly(disulfide)s: the dependence of activity, depolymerization kinetics and intracellular localization on their length“ Org. Biomol. Chem. 2015, 13:64-7. [DOI]
E. Schönhofer, B. Bozic-Weber, C. J. Martin, E. C. Constable, C. E. Housecroft, J. A. Zampese “‘Surfaces-as-ligands, surfaces-as-complexes’ strategies for copper(I) dye-sensitized solar cells“ Dyes Pigm. 2015, 115:154. [DOI]
T. Schuster, M. Nussbaumer, P. Baumann, N. Bruns, W. Meier, A. Car “Polymeric particulates for subunit vaccine delivery“ Subunit Vaccine Delivery 2015:181-201. [DOI]
D. Alsteens, S. Tay, D. J. Müller “Toward high-throughput biomechanical phenotyping of single molecules“ Nat. Methods 2015, 12:45. [DOI]
G. Gunkel-Grabole, S. Sigg, M. Lomora, S. Lörcher, C. G. PalivanW. Meier “Polymeric 3D nano-architectures for transport and delivery of therapeutically relevant biomacromolecules“ Biomater. Sci. 2015, 2:25. [DOI]
A. Najer, D. Wu, A. Bieri, F. Brand, C. G. Palivan, H. P. Beck, W. Meier “Nanomimics of Host Cell Membranes Block Invasion and Expose Invasive Malaria Parasites“ ACS Nano 2014, 8:12560. [DOI] [More Information]
F. Itel, M. Chami, A. Najer, S. Lörcher, D. Wu, I. A. Dinu, W. Meier “Molecular organization and dynamics in polymersome membranes: A lateral diffusion study“ Macromolecules 2014, 47:7588. [DOI]
T. Szikra, S. Trenholm, A. Drinnenberg, J. Jüttner, Z. Raics, K. Farrow, M. Biel, G. Awatramani, D. A. Clark, J. A. Sahel, R. Azeredo da Silveira, B. Roska “Rods in daylight act as relay cells for cone-driven horizontal cell–mediated surround inhibition“ Nat. Neurosci. 2014, 17:1728. [DOI]
K. Fujisawa, C. Beuchat, M. Humbert-Droz, A. Wilson, T. A. Wesolowski, J. Mareda, N. Sakai, S. Matile “Anion-π and cation-π interactions on the same surface“ Angew. Chem. Int. Ed. 2014, 53:11266-9. [DOI]
D. Steuerwald, S. M. Fruh, R. Griss, R. D. Lovchik, V. Vogel “Nanoshuttles propelled by motor proteins sequentially assemble molecular cargo in a microfluidic device“ Lab Chip 2014, 14:3729-38. [DOI]
F. N. Miros, G. Huang, Y. Zhao, N. Sakai, S. Matile “Coumarin synthesis on π-acidic surfaces“ Supramol. Chem. 2014, 27:303-09. [DOI]
K. Yonehara, B. Roska “Neuroscience: retinal projectome reveals organizing principles of the visual system“ Curr. Biol. 2014, 24:R833-5. [DOI]
H. Hayashi, A. Sobczuk, A. Bolag, N. Sakai, S. Matile “Antiparallel three-component gradients in double-channel surface architectures“ Chem. Sci. 2014, 5:4610-14. [DOI]
D. Wu, M. Spulber, F. Itel, M. Chami, T. Pfohl, C. G. PalivanW. Meier “Effect of Molecular Parameters on the Architecture and Membrane Properties of 3D Assemblies of Amphiphilic Copolymers“ Macromolecules 2014, 47:5060-69. [DOI]
T. Cronin, L. H. Vandenberghe, P. Hantz, J. Juttner, A. Reimann, A. E. Kacsó, R. M. Huckfeldt, V. Busskamp, H. Kohler, P. S. Lagali, B. Roska, J. Bennett “Efficient transduction and optogenetic stimulation of retinal bipolar cells by a synthetic adeno-associated virus capsid and promoter“ EMBO Mol. Med. 2014, 6:1175. [DOI]
P. Baumann, M. Spulber, I. A. Dinu, C. G. Palivan “Cellular Trojan Horse Based Polymer Nanoreactors with Light-sensitive Activity“ J. Phys. Chem. B 2014, 118:9361. [DOI]
A. S. Chuong, M. L. Miri, V. Busskamp, G. A. C. Matthews, L. C. Acker, A. T. Sørensen, A. Young, N. C. Klapoetke, M. A. Henninger, S. B. Kodandaramaiah, M. Ogawa, S. B. Ramanlal, R. C. Bandler, B. D. Allen, C. R. Forest, B. Y. Chow, X. Han, Y. Lin, K. M. The, B. Roska, J. A. Cardin, E. S. Boyden “Noninvasive optical inhibition with a red-shifted microbial rhodopsin “ Nat. Neurosci. 2014, 17:1123. [DOI]
V. Busskamp, J. Krol, D. Nelidova, J. Daum, T. Szikra, B. Tsuda, J. Jüttner, K. Farrow, B. Gross Scherf, C. P. Patino Alvarez, C. Genoud, V. Sothilingam, N. Tanimoto, M. Stadler, M. Seeliger, M. Stoffel, W. Filipowicz, B. Roska “miRNAs 182 and 183 Are Necessary to Maintain Adult Cone Photoreceptor Outer Segments and Visual Function“ Neuron 2014, 83:586. [DOI]
R. A. Kellogg, R. Gomez-Sjoberg, A. A. Leyrat, S. Tay “High-throughput microfluidic single-cell analysis pipeline for studies of signaling dynamics“ Nat. Protoc. 2014, 9:1713-26. [DOI]
K. D. Schleicher, S. L. Dettmer, L. E. Kapinos, S. Pagliara, U. F. Keyser, S. Jeney, R. Y. H. Lim “Selective transport control on molecular velcro made from intrinsically disordered proteins“ Nat. Nanotechnol. 2014, 9:525. [DOI]
A. V. Jentzsch, S. Matile “Anion transport with halogen bonds“ Halogen Bonding I 2014:205-39. [DOI]

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Project management Persons involved [grouplink]
Randall Platt Mariia Cherepkova
Maria Kuhn
Sushmita Poddar
Antonio Santinha
Florian Schmidt
Niels Weisbach

Platt group @D-BSSE

Florian Seebeck Alice Maurer

Seebeck group @UniBas

Ivan Martin
Yaakov Benenson
Manuele Giuseppe Muraro

Martin group @UniBas

Benenson group @D-BSSE

Catherine E. Housecroft
Cornelia G. Palivan
Myrto Kyropoulou
Dalin Wu

Housecroft group @UniBas

Palivan group @UniBas

Florian Seebeck
Petra Dittrich

Seebeck group @UniBas

Dittrich group @D-BSSE

Wolfgang Meier
Martin Fussenegger

Meier group @UniBas

Fussenegger group @D-BSSE

Jonathan De Roo N.N.

De Roo group @UniBas

Marcel Mayor
Emanuel Lörtscher

Mayor group @UniBas

Lörtscher group @IBM

Christof Sparr Daniel Moser
Felix Raps
Dragan Miladinov
Zlatko Joncev

Sparr group @UniBas

Marcel Mayor Marius Ciobanu
Tim Hohner
Gabriel Puebla-Hellman
David Vogel
Giulia Prone

Mayor group @UniBas

Konrad Tiefenbacher
Cornelia G. Palivan

Tiefenbacher group @UniBas

Palivan group @UniBas

Sven Panke Daniel Gerngross
Lukas Huber
Markus Jeschek
Eirini Rousounelou
Peter Ruppen
Sanja Tunjic

Panke group @D-BSSE

Dimitrios Fotiadis Stephan Hirschi
Mirko Stauffer

Fotiadis group @UniBe

Botond Roska Jacek Krol
Magdalena Renner
Tamas Szikra

Roska group @FMI

Bruno Correia
Sai Reddy
Pablo Gainza

Correia group @EPFL

Reddy group @D-BSSE

Dimitrios Fotiadis
Wolfgang Meier
Daniel J. Müller

Fotiadis group @UniBe

Meier group @UniBas

Müller group @D-BSSE

Nikola Biller-Andorno Sebastian Wäscher

Biller-Andorno group @UniZH

Sai Reddy Theresa Pesch
Derek Mason
Jakub Kucharczyk

Reddy group @D-BSSE

Sai Reddy
Thomas R. Ward

Reddy group @D-BSSE

Ward group @UniBas

Oliver Wenger Mirjam Schreier
Jasmin Anastasia Kübler
Christopher Bryan Larsen

Wenger group @UniBas