press information / news

News from HMGU
09.11.2017

Nobel Prize laureate Robert Huber visits the Helmholtz Zentrum München

On 8 November 2017, the Munich-born Nobel laureate Robert Huber was a guest of the Helmholtz Zentrum München. The occasion was the mid-term review of AEGIS (Accelerated Early stage drug dIScovery), an EU-wide research project coordinated by the Institute of Structural Biology (STB) at the Helmholtz Zentrum München as part of the Horizon 2020 program. Professor Huber, who was awarded the Nobel Prize for Chemistry in 1988, outlined the history of structural biology research to his large audience and took an optimistic view of the future.

Source: Helmholtz Zentrum München

In his lecture, Professor Huber focused on the significance of the three-dimensional structure of biological macromolecules in drug development. Under the heading “New ways of vision: protein structures in translational medicine and business development – My experience”, he spanned the whole spectrum – from the beginnings of X-ray crystallography to the latest nuclear magnetic resonance (NMR) spectroscopy techniques. Citing several examples, he went on to explain how the unveiling of biological structures can frequently lead to very specific applications. One such example was the decoding of natural inhibitors of the blood-thinning factor thrombin (found, for example, in leeches), which played a pioneering role in the development of certain anticoagulants. In the field of diabetes, Huber cited the unraveling of the spatial structure of the enzyme DPP4, which led to the development of several DPP4 inhibitors. Turning to the future, he explained that, increasingly, attention is focusing on the proteasome as a particularly interesting structure for the development of new antibiotics.

“Our first protein models were still made of wire and screws”

Asked about the new possibilities opening up in structural research, for instance in the framework of the Bavarian NMR Center, which is operated by the Helmholtz Zentrum München and the Technical University of Munich (TUM), Huber replied: “These new technologies are fantastic! Hardly any of the instruments and methods that are now well established and enable us to go much deeper were available to us back in our day. Just look at cryo-electron microscopy. We are currently experiencing a revolution in that field that would have been inconceivable a few years ago.” Huber said he could even imagine molecular structures being predicted by computers in the future, thanks to ever-improving algorithms and models.

Three generations of research into active substances

STB director and AEGIS coordinator Professor Michael Sattler expressed a similar view: “Thanks to integrative structural biology, which encompasses various methods such as X-ray structural analysis, NMR spectroscopy and cryo-electron microscopy as well as computer-aided molecular dynamics and theoretical chemistry, superb opportunities are emerging nowadays!” He was therefore delighted to have the opportunity at the gathering in Munich to bring together three generations of scientists engaged in active substance research and to pave the way for future collaboration and publications. With reference to the younger members of the audience, Huber gave the following advice to the up-and-coming generation: “Besides the passion, the power and the commitment that you need in order to have a successful career in science, it is important to recognize your own path. Choose the field you would like to enter and seek a mentor who will not only encourage you, but also give you the necessary freedom!”


Further Information


Background:
In 1988, Robert Huber was awarded the Nobel Prize in Chemistry “for the determination of the three-dimensional structure of a photosynthetic reaction center” together with Hartmut Michel and Johann Deisenhofer. He studied, did his doctorate and post-doctoral qualification as professor in chemistry at the TUM, to which he remained attached as director of the Max Planck Institute for Biochemistry. He had already begun to focus on crystallography for his dissertation, and he had established a protein crystallography laboratory in the early 1970s. Over the years, with the help of X-ray crystallography, he was able to demonstrate the structure of numerous proteins and protein complexes, including protease and their natural and synthetic inhibitors; metalloenzymes; immune system proteins; protein hormones and their receptors; protein kinases; amino acid biosynthesis enzymes; and energy and electron transfer proteins. Moreover, he developed and improved new devices and methods now standard in X-ray structural analysis – for example, the Patterson Method, graphic methods and the improvement of protein crystallization. Robert Huber is also co-founder of the biotech companies Proteros and Suppremol and a member of the academic advisory board of the Peter and Traudl Engelhorn Stiftung as well as several pharmaceutical companies. Additionally, he is member of Bayerischen Akademie der Wissenschaften, Deutschen Akademie der Naturforscher Leopoldina and Academia Europaea, last but not least he keeps quite a number of guest professorships all over the world. Robert Huber continues to conduct research at the Max Planck Institute of Biochemistry up to the present day.

The AEGIS (Accelerated Early staGe drug dIScovery) project is dedicated to developing innovative bioactive compounds targeting neglected diseases, such as African Sleeping sickness, Chagas’ disease or tuberculosis, and to training talented researchers in this area. The project, which has funding of 3.84 million euros, is coordinated by Prof. Dr. Michael Sattler, Director of the Institute of Structural Biology (STB) at the Helmholtz Zentrum München. The project brings together eleven partners from industrial and academic research institutions in seven European countries. In addition, 16 partner organizations are participating in the project. The goal of these researchers is to exploit the three-dimensional structure of proteins to develop and apply innovative procedures for the design of small molecules that target protein interaction to eventually eliminate pathogens.

As German Research Center for Environmental Health, Helmholtz Zentrum München pursues the goal of developing personalized medical approaches for the prevention and therapy of major common diseases such as diabetes mellitus and lung diseases. To achieve this, it investigates the interaction of genetics, environmental factors and lifestyle. The Helmholtz Zentrum München has about 2,300 staff members and is headquartered in Neuherberg in the north of Munich. Helmholtz Zentrum München is a member of the Helmholtz Association, a community of 18 scientific-technical and medical-biological research centers with a total of about 37,000 staff members. 

The Institute for Structural Biology (STB) investigates the spatial structures of biological macromolecules, their molecular interactions and dynamics using integrated structural biology by combining X-ray crystallography, NMR-spectroscopy and other methods. Researchers at STB also develop NMR spectroscopy methods for these studies. The goal is to unravel the structural and molecular mechanisms underlying biological function and their impairment in disease. The structural information is used for the rational design and development of small molecular inhibitors in combination with chemical biology approaches.