Press releases – November 2020

 

Nov 24 2020
10:56

Federal and state funding of € 9.2 million for a long-term academy project at Goethe University and Friedrich Schiller University Jena 

24 years for Buber research in the digital age

Approximately 40,000 letters from Martin Buber’s correspondence with his contemporaries exist, but to this day, they have hardly been accessible. A funding commitment from the federal and state governments should now change this: an academy project for the digitalisation and annotation of this valuable estate will be funded with almost € 400,000 per year.

FRANKFURT. Literature, art, theology – Martin Buber, one of the most influential thinkers of the modern German-Jewish intellectual world was in active exchange with the representatives and institutions in almost every area of intellectual life. More than 40,000 letters that were written by or to him have been handed down – particularly in the philosopher’s estate in Jerusalem, but also scattered throughout archives around the world. Making this research treasure accessible – that is the goal of the new academy project that Professor Christian Wiese, scholar in the field of Jewish Studies and holder of the Martin-Buber-Chair in Jewish Religious Philosophy at Goethe University, can now tackle thanks to the funds awarded by the federal and state governments. All the letters are to be digitalised as facsimile, and a large portion will also be transcribed, translated and annotated. The project is designed for 24 years and will be funded with € 9.2 million, of which half will come from the Federal Ministry of Education and Research and half from the Hessian Ministry of Higher Education, Research and the Arts. Professor Martin Leiner (Friedrich Schiller University Jena), Professor Abigail Gilman (Boston University) and the National Library of Israel are cooperation partners.

“This is wonderful news.” Professor Birgitta Wolff, President of Goethe University, is delighted about the grant. “With this academy project, Christian Wiese is setting new standards and planting the seed for a work that fits the time in every way,” Wolff remarks, adding that the project is an important contribution to internationalisation in the digital humanities. “It is in fact quite special. There is nothing like it in other countries,” says Professor Christian Wiese, who in 2019 concluded one of the last volumes of the edition of Martin Buber’s published writings. The edition of the letters opens additional perspectives into Buber’s life and work and his many interests – but also into intellectual life overall in the decades between the first World War and Buber’s death in 1965. “Where, if not in Frankfurt, should this project have its home?” observes Wiese.

“The correspondence of Buber, who lived in Heppenheim and taught in Frankfurt, can contribute important new insights to the history of the twentieth century. Especially in our polarised time, we can learn a lot from the philosopher’s approach, which always relied on dialogue and understanding. Christian Wiese’s academy project is for this reason also an exceptional one in Hessen’s research landscape in the humanities. I am very happy that we can co-fund this project and wish it great success,” says Hessen’s minister for Higher Education, Research and the Arts Angela Dorn.

Martin Buber (1868 – 1965) worked at the University of Frankfurt am Main from 1924 to 1933 – first as lecturer and later as honorary professor for Jewish religious teachings and ethics. He resigned from the professorship in 1933 after Hitler took power in anticipation of having his professorship revoked. He subsequently worked on setting up the Central Office for Jewish Adult Education with the Reichsvertretung of German Jews until it was forced to give up its work. Buber emigrated to Israel in 1938 before the November pogrom. Throughout his entire life, Martin Buber was in contact with personalities from all areas of intellectual life, including many writers such as Margarete Susman, Hermann Hesse, Arnold Zweig, Thomas Mann and Franz Kafka. Here, he did not shy away from controversial discussions. “The letters are a fascinating mirror of the time and reveal the intellectual network in which Buber was involved,” says Christian Wiese. Perhaps a quarter of the letters were written by Martin Buber; the rest were written to him. But Martin Buber’s personality and thought are reflected in these as well.

As part of the project, the letters, which are primarily located in Europe, Israel and the USA, are now to be collected and grouped according to thematic modules that stretch over several years, and made digitally accessible in close collaboration with the Academy of Sciences and Literature in Mainz. Depending on the content, transcripts and – where necessary – translations from the Hebrew along with annotations will be added. The academy project provides for three editorial positions and a doctoral scholarship. Annual conferences are planned, as well as intensive cooperation with researchers in Israel and the USA. The positions will be advertised soon so that work can start in the spring.

“Martin Buber and his work are more relevant than ever,“ says Professor Wiese with conviction. “He is one of the most important dialogic thinkers of the twentieth century, and his texts are relevant wherever intercultural or interreligious dialogue takes place. At the same time, they possess great meaning for issues of political ethics.”

Images may be downloaded here:  http://www.uni-frankfurt.de/94469362

Caption: This letter to Hermann Hesse was written on 16 September 1945, the day after Yom Kippur, and is the first letter that the philosopher sent from Jerusalem to Germany after the war and the Shoah.

Further information
Prof. Dr. Christian Wiese
Martin Buber Chair for Jewish Religious Philosophy
Faculty 06
Goethe University
Phone: +49 69 798-33313
E-Mail c.wiese@em.uni-frankfurt.de
Internet: https://www.uni-frankfurt.de/40998908/Profil


 

Nov 23 2020
15:55

Research cooperation between Goethe University, University of Kent and the Hannover Medical School

The drug aprotinin inhibits entry of SARS-CoV2 in host cells

In order for the SARS-CoV2 virus to enter host cells, its “spike" protein has to be cleaved by the cell's own enzymes - proteases. The protease inhibitor aprotinin can prevent cell infection, as scientists at Goethe University, the University of Kent and the Hannover Medical School have now discovered. An aprotinin aerosol is already approved in Russia for the treatment of influenza and could readily be tested for the treatment of COVID-19.

FRANKFURT. The surface of the SARS-CoV-2 virus is studded with spike proteins. The virus needs these in order to dock onto proteins (ACE2 receptors) on the surface of the host cell. Before this docking is possible, parts of the spike protein have to be cleaved by the host cell's enzymes – proteases.

In cell culture experiments with various cell types, the international scientific team led by Professor Jindrich Cinatl, Institute for Medical Virology at the University Hospital Frankfurt, Professor Martin Michaelis, and Dr Mark Wass (both University of Kent) demonstrated that the protease inhibitor aprotinin can inhibit virus replication by preventing SARS-CoV2 entry into host cells. Moreover, aprotinin appears to compensate for a SARS-CoV2-induced reduction of endogenous protease inhibitors in virus-infected cells.

Influenza viruses require host cell proteases for cell entry in a similar way as coronaviruses. Hence, an aprotinin aerosol is already approved in Russia for the treatment of influenza.

Professor Jindrich Cinatl said: “Our findings show that aprotinin is effective against SARS-CoV2 in concentrations that can be achieved in patients. In aprotinin we have a drug candidate for the treatment of COVID-19 that is already approved for other indications and could readily be tested in patients."

Publication: Denisa Bojkova, Marco Bechtel, Katie-May McLaughlin, Jake E. McGreig, Kevin Klann, Carla Bellinghausen, Gernot Rohde, Danny Jonigk, Peter Braubach, Sandra Ciesek, Christian Münch, Mark N. Wass, Martin Michaelis, Jindrich Cinatl jr. Aprotinin inhibits SARS-CoV-2 replication. Cells 2020, https://www.mdpi.com/2073-4409/9/11/2377

Further information:
Professor Dr. rer. nat. Jindrich Cinatl
Institute for Medical Virology
University Hospital Frankfurt am Main
Tel. +49 69 6301-6409
cinatl@em.uni-frankfurt.de
https://www.kgu.de/einrichtungen/institute/zentrum-der-hygiene/medizinische-virologie/forschung/research-group-cinatl/

 

Nov 20 2020
10:41

​Scientists at Goethe University within the international consortium COVID19-NMR refine previous 2D models

Folding of SARS-CoV2 genome reveals drug targets – and preparation for “SARS-CoV3”

For the first time, an international research alliance has observed the RNA folding structures of the SARS-CoV2 genome with which the virus controls the infection process. Since these structures are very similar among various beta corona viruses, the scientists not only laid the foundation for the targeted development of novel drugs for treating COVID-19, but also for future occurrences of infection with new corona viruses that may develop in the future.

FRANKFURT. The genetic code of the SARS-CoV2 virus is exactly 29,902 characters long, strung through a long RNA molecule. It contains the information for the production of 27 proteins. This is not much compared to the possible 40,000 kinds of protein that a human cell can produce. Viruses, however, use the metabolic processes of their host cells to multiply. Crucial to this strategy is that viruses can precisely control the synthesis of their own proteins.

SARS-CoV2 uses the spatial folding of its RNA hereditary molecule as control element for the production of proteins: predominantly in areas that do not code for the viral proteins, RNA single strands adopt structures with RNA double strand sections and loops. However, until now the only models of these foldings have been based on computer analyses and indirect experimental evidence.

Now, an international team of scientists led by chemists and biochemists at Goethe University and TU Darmstadt have experimentally tested the models for the first time. Researchers from the Israeli Weizmann Institute of Science, the Swedish Karolinska Institute and the Catholic University of Valencia were also involved.

The researchers were able to characterise the structure of a total of 15 of these regulatory elements. To do so, they used nuclear magnetic resonance (NMR) spectroscopy in which the atoms of the RNA are exposed to a strong magnetic field, and thereby reveal something about their spatial arrangement. They compared the findings from this method with the findings from a chemical process (dimethyl sulphate footprint) which allows RNA single strand regions to be distinguished from RNA double strand regions.

The coordinator of the consortium, Professor Harald Schwalbe from the Center for Biomolecular Magnetic Resonance at Goethe University Frankfurt, explains: “Our findings have laid a broad foundation for future understanding of how exactly SARS-CoV2 controls the infection process. Scientifically, this was a huge, very labour-intensive effort which we were only able to accomplish because of the extraordinary commitment of the teams here in Frankfurt and Darmstadt together with our partners in the COVID-19-NMR consortium. But the work goes on: together with our partners, we are currently investigating which viral proteins and which proteins of the human host cells interact with the folded regulatory regions of the RNA, and whether this may result in therapeutic approaches."

Worldwide, over 40 working groups with 200 scientists are conducting research within the COVID-19-NMR consortium, including 45 doctoral and postdoctoral students in Frankfurt working in two shifts per day, seven days of the week since the end of March 2020.

Schwalbe is convinced that the potential for discovery goes beyond new therapeutic options for infections with SARS-CoV2: “The control regions of viral RNA whose structure we examined are, for example, almost identical for SARS-CoV and also very similar for other beta-coronaviruses. For this reason, we hope that we can contribute to being better prepared for future 'SARS-CoV3' viruses."

The Center for Biomolecular Magnetic Resonance was founded in 2002 as research infrastructure at Goethe University Frankfurt and has since then received substantial funding from the State of Hessen.

Publication: Anna Wacker, Julia E. Weigand, Sabine R. Akabayov, Nadide Altincekic, Jasleen Kaur Bains, Elnaz Banijamali, Oliver Binas, Jesus Castillo-Martinez, Erhan Cetiner, Betül Ceylan, Liang-Yuan Chiu, Jesse Davila-Calderon, Karthikeyan Dhamotharan, Elke Duchardt-Ferner, Jan Ferner, Lucio Frydman, Boris Fürtig, José Gallego, J. Tassilo Grün, Carolin Hacker, Christina Haddad, Martin Hähnke, Martin Hengesbach, Fabian Hiller, Katharina F. Hohmann, Daniel Hymon, Vanessa de Jesus, Henry Jonker, Heiko Keller, Bozana Knezic, Tom Landgraf, Frank Löhr, Le Luo, Klara R. Mertinkus, Christina Muhs, Mihajlo Novakovic, Andreas Oxenfarth, Martina Palomino-Schätzlein, Katja Petzold, Stephen A. Peter, Dennis J. Pyper, Nusrat S. Qureshi, Magdalena Riad, Christian Richter, Krishna Saxena, Tatjana Schamber, Tali Scherf, Judith Schlagnitweit, Andreas Schlundt, Robbin Schnieders, Harald Schwalbe, Alvaro Simba-Lahuasi, Sridhar Sreeramulu, Elke Stirnal, Alexey Sudakov, Jan-Niklas Tants, Blanton S. Tolbert, Jennifer Vögele, Lena Weiß, Julia Wirmer-Bartoschek, Maria A. Wirtz Martin, Jens Wöhnert, Heidi Zetzsche: Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy. Nucleic Acids Research, 2020, https://academic.oup.com/nar/advance-article/doi/10.1093/nar/gkaa1013/5961789

Image download: http://www.uni-frankfurt.de/94413328

Caption: Regulatory RNA elements of the SARS-CoV2 genome. Black: regions not coding for proteins (UTR); orange: coding regions (ORF).

Further information

Prof. Dr. Harald Schwalbe

Institute for Chemistry and Chemical Biology 
Center for Biomolecular Magnetic Resonance (BMRZ)

Goethe University Frankfurt
Tel +49 69 798-29137
schwalbe@nmr.uni-frankfurt.de
http://schwalbe.org.chemie.uni-frankfurt.de/

 

Nov 13 2020
11:45

Chemists at the University of Göttingen and Goethe University Frankfurt characterise key compound for catalytic nitrogen atom transfer

Chemistry: How nitrogen is transferred by a catalyst

Catalysts with a metal-nitrogen bond can transfer nitrogen to organic molecules. In this process short-lived molecular species are formed, whose properties critically determine the course of the reaction and product formation. The key compound in a catalytic nitrogen-atom transfer reaction has now been analysed in detail by chemists at the University of Göttingen and Goethe University Frankfurt. The detailed understanding of this reaction will allow for the design of catalysts tailored for specific reactions.

FRANKFURT. The development of new drugs or innovative molecular materials with new properties requires specific modification of molecules. Selectivity control in these chemical transformations is one of the main goals of catalysis. This is particularly true for complex molecules with multiple reactive sites in order to avoid unnecessary waste for improved sustainability. The selective insertion of individual nitrogen atoms into carbon-hydrogen bonds of target molecules is, for instance, a particularly interesting goal of chemical synthesis. In the past, these kinds of nitrogen transfer reactions were postulated based on quantum-chemical computer simulations for molecular metal complexes with individual nitrogen atoms bound to the metal. These highly reactive intermediates have, however, previously escaped experimental observation. A closely entangled combination of experimental and theoretical studies is thus indispensable for detailed analysis of these metallonitrene key intermediates and, ultimately, the exploitation of catalytic nitrogen-atom transfer reactions.

Chemists in the groups of Professor Sven Schneider, University of Göttingen, and Professor Max Holthausen, Goethe University Frankfurt, in collaboration with the groups of Professor Joris van Slagern, University of Stuttgart and Professor Bas de Bruin, University of Amsterdam, have now been able for the first time to directly observe such a metallonitrene, measure it spectroscopically and provide a comprehensive quantum-chemical characterization. To this end, a platinum azide complex was transformed photochemically into a metallonitrene and examined both magnetometrically and using photo-crystallography. Together with theoretical modelling, the researchers have now provided a detailed report on a very reactive metallonitrene diradical with a single metal-nitrogen bond. The group was furthermore able to show how the unusual electronic structure of the platinum metallonitrene allows the targeted insertion of the nitrogen atom into, for example, C–H bonds of other molecules.

Professor Max Holthausen explains: “The findings of our work significantly extend the basic understanding of chemical bonding and reactivity of such metal complexes, providing the basis for a rational synthesis planning.” Professor Sven Schneider says: “These insertion reactions allow the use of metallonitrenes for the selective synthesis of organic nitrogen compounds through catalyst nitrogen atom transfer. This work therefore contributes to the development of novel ‘green’ syntheses of nitrogen compounds.”

The research was funded by the Deutsche Forschungsgemeinschaft and the European Research Council.

Publication: Jian Sun, Josh Abbenseth, Hendrik Verplancke, Martin Diefenbach, Bas de Bruin, David Hunger, Christian Würtele, Joris van Slageren, Max C. Holthausen, Sven Schneider: A platinum(II) metallonitrene with a triplet ground state. Nat. Chem. (2020) https://doi.org/10.1038/s41557-020-0522-4

Further information:
Prof. Dr. Max C. Holthausen
Goethe University Frankfurt am Main
Institute for Inorganic and Analytical Chemistry
Tel. +49 69 798 29430
max.holthausen@chemie.uni-frankfurt.de

Prof. Dr. Sven Schneider
Georg-August-Universität Göttingen
Institute for Inorganic Chemistry
Tel. +49 551 39 22829
sven.schneider@chemie.uni-goettingen.de

 

Nov 12 2020
13:53

Synthetic vesicles are mini-laboratories for customised molecules

Researchers at Goethe University create artificial cell organelles for biotechnology 

Cells of higher organisms use cell organelles to separate metabolic processes from each other. This is how cell respiration takes place in the mitochondria, the cell's power plants. They can be compared to sealed laboratory rooms in the large factory of the cell. A research team at Goethe University has now succeeded in creating artificial cell organelles and using them for their own devised biochemical reactions.

FRANKFURT. Biotechnologists have been attempting to “reprogram" natural cell organelles for other processes for some time – with mixed results, since the “laboratory equipment" is specialised on the function of organelles. Dr Joanna Tripp, early career researcher at the Institute for Molecular Biosciences has now developed a new method to produce artificial organelles in living yeast cells (ACS Synthetic Biology: https://doi.org/10.1021/acssynbio.0c00241).

To this end, she used the ramified system of tubes and bubbles in the endoplasmic reticulum (ER) that surrounds the nucleus.  Cells continually tie off bubbles, or vesicles, from this membrane system in order to transport substances to the cell membrane. In plants, these vesicles may also be used for the storage of proteins in seeds. These storage proteins are equipped with an “address label" – the Zera sequence – which guides them to the ER and which ensures that storage proteins are “packaged" there in the vesicle. Joanna Tripp has now used the “address label" Zera to produce targeted vesicles in yeast cells and introduce several enzymes of a biochemical metabolic pathway.

This represents a milestone from a biotechnical perspective. Yeast cells, the “pets" of synthetic biology not only produce numerous useful natural substances, but can also be genetically changed to produce industrially interesting molecules on a grand scale, such as biofuels or anti-malaria medicine.

In addition to the desired products, however, undesirable by-products or toxic intermediates often occur as well. Furthermore, the product can be lost due to leaks in the cell, or reactions can be too slow. Synthetic cell organelles offer remedies, with only the desired enzymes (with “address labels") encountering each other, so that they work together more effectively without disrupting the rest of the cell, or being disrupted themselves.

“We used the Zera sequence to introduce a three-stage, synthetic metabolic pathway into vesicles," Joanna Tripp explains. “We have thus created a reaction space containing exactly what we want. We were able to demonstrate that the metabolic pathway in the vesicles functions in isolation to the rest of the cell."

The biotechnologist selected an industrially relevant molecule for this process: muconic acid, which is further processed industrially to adipic acid. This is an intermediate for nylon and other synthetic materials. Muconic acid is currently won from raw oil. A future large-scale production using yeast cells would be significantly more environment-friendly and sustainable. Although a portion of the intermediate protocatechuic acid is lost because the vesicle membrane is porous, Joanna Tripp views this as a solvable problem.

Professor Eckhard Boles, Head of the Department of Physiology and Genetics of Lower Eukaryotes observes: “This is a revolutionary new method of synthetic biology. With the novel artificial organelles, we now have the option of generating various processes in the cell anew, or to optimise them." The method is not limited to yeast cells, but can be utilised for eukaryotic cells in general. It can also be applied to other issues, e.g. for reactions that have previously not been able to take place in living cells because they may require enzymes that would disrupt the cell metabolic process.

Publication: Mara Reifenrath, Mislav Oreb, Eckhard Boles, Joanna Tripp: Artificial ER-Derived Vesicles as Synthetic Organelles for in Vivo Compartmentalization of Biochemical Pathways, in:
ACS Synthetic Biology: https://doi.org/10.1021/acssynbio.0c00241

Further information:
Dr. Joanna Tripp
Institute for Molecular Biosciences
Goethe University Frankfurt
Tel.: + 49 69 798 29516 
j.tripp@bio.uni-frankfurt.de