Biology

Researchers at the Paul Scherrer Institute PSI have elucidated an important part of a siganalling pathway that transmits information through the cell membrane into the interior of a cell. This exists in all mammals and plays an important role, among other things, in the regulation of the heartbeat. The new findings could lead to new therapies.

For the development of new medicinal agents, accurate knowledge of proteins is crucial. In a pilot experiment, researchers have now, for the first time, used the X-ray free-electron laser SwissFEL of PSI for the examination of protein crystals.

Gebhard Schertler is head of the research division Biology and Chemistry at the Paul Scherrer Institute PSI and professor for Structural Biology at ETH Zurich. In this interview he talks about biological research at PSI and the future of drug development.

Using X-ray laser technology, a team led by researchers of the Paul Scherrer Institute PSI has recorded one of the fastest processes in biology. In doing so, they produced a molecular movie that reveals how the light sensor retinal is activated in a protein molecule. Such reactions occur in numerous organisms. The movie shows for the first time how a protein efficiently controls the reaction of the embedded light sensor.

With the X-ray laser SwissFEL, researchers at PSI want to produce movies of biomolecules in action. This can reveal how our eyes function or how new drugs work.

The 16th of May is the International Day of Light. The research carried out with light at PSI enables advances in biology and pharmacology and also promotes the development of new materials for data storage and new technologies for personalised medicine.

With a new method for modifying antibodies, Philipp Spycher, winner of a Founder Fellowship at the Paul Scherrer Institute PSI, wants to develop drugs that are more stable and, thus, have fewer side-effects.

With the new Founder Fellowship, the Paul Scherrer Institute PSI gives young researchers the chance to become entrepreneurs. Within 18 months they have to demonstrate the commercialisation potential of their business ideas and draw up an initial business plan. Today the official ceremony awarding this grant took place: The first three prize winners are working on a new pharmaceutical technology, a nano-energy technology, and a neutron detector.

The Nobel Prize in Chemistry 2017 has been awarded to Jacques Dubochet of Switzerland, U.S.-based German scientist Joachim Frank, and Richard Henderson of the United Kingdom for the development of structural analysis of single biological molecules by means of cryo-electron microscopy. The awarding of the prize underscores the fundamental significance of structural analysis of biomolecules for modern biology – a research area where the Paul Scherrer Institute PSI plays a leading role in Switzerland.

A pharmaceuticals manager at Roche for a long time, now he is the founder of a biotech firm on the campus of the Paul Scherrer Institute PSI: Michael Hennig knows the trends in the medical sector. In this interview he explains why the medicine of the future needs the innovation power of publicly funded research, and why he chose to locate his start-up leadXpro so close to PSI.

Martin Ostermaier wanted to break out of the comfort zone of science. Now, instead of pipettes, the biochemist is dealing with investors and patent law.

Proteins are indispensable building blocks of life. They play a vital role in many biological processes. Researchers have now been able to show how the ultrafast processes by which proteins do their work can be studied with free-electron X-ray lasers such as SwissFEL at the Paul Scherrer Institute PSI. Free-electron X-ray lasers generate extremely short and intense pulses of X-ray light. Currently there are just two such facilities in operation, worldwide. The results were published in the scientific journal Nature Communications.

PSI researcher Kurt Ballmer-Hofer is concerned with the question of how tumours could be starved by preventing the development of blood vessels. After 40 years of research that yielded many fundamental insights about the formation of blood vessels, one of the key molecules has been found; further research is expected to enable clinical applications.

At the PSI, the exact structure of proteins is deciphered in the standard way, with X-rays. Now two PSI researchers have used a clever trick to advance this method further: Instead of pinning down the proteins, they are studying them within a levitating drop of liquid.

New insights into the workings of important drug receptorsMany medical drugs operate on specific receptors located in the outer walls of our body’s cells. One of these is called the beta-1 adrenergic receptor. Among other things, it is responsible for palpitation, the racing pulse that we feel with stage fright or infatuation. How it transmits signals to the cellular interior can now be revealed in detail. These findings could help scientists better understand many drugs' mode of action.

Bones are made up of tiny fibres that are roughly a thousand times finer than a human hair. Researchers at the Paul Scherrer Institute PSI have developed a new computer-based algorithm with which they were able to visualize the localised order and alignment of these nanostructures inside an entire piece of bone for the first time.

The Paul Scherrer Institute PSI is involved in a project conducted by several research institutes (spearheaded by EPFL) to devise an X-ray machine especially for developing countries. The device should be able to cope with tropical climes and be easy and cheap to repair. PSI researchers are focusing on producing a cost-effective detector that is necessary for the imaging. The detector registers the X-ray light much like a chip in a digital camera.

Researchers unveil new details of how cells in a living organism process stimuli. So-called G-proteins, which help conduct external stimuli that reach a cell into its interior, play a central role here. For the first time, the study shows which parts of the G-proteins are vital for their function. Researchers from the Paul Scherrer Institute PSI, ETH Zurich, the pharmaceutical company Roche and the British MRC Laboratory of Molecular Biology report their results in the journals Nature and Nature Structural and Molecular Biology.

All living organisms, from bacteria to humans, rely on proteins to perform their vital functions. How these proteins accomplish their tasks depends on their structure. Researchers from the Paul Scherrer Institute have now devised a novel method to determine the crystal structure of proteins using X-ray light, which could also hasten the development of new drugs in future. The study will be published in the journal Nature Methods on 15 December.

The way that algae and plants respond to light has been reinterpreted based on results from recent experiments. Under particular lighting conditions during photosynthesis, the well-ordered stacking and alignment of light-sensitive membranes in the algae are disrupted. There is no significant movement of the membrane embedded light harvesting proteins, which rather become largely inactive. These new findings challenge widely accepted views of how algae respond to light where the light harvesting proteins were thought to move around the membranes.