Nordic Life Science 1
INTERV IEW LIDDS CAGLA SAHIN’S RESEARCH focuses o
n expanding our knowledge of how the human memory is formed and stored. She will investigate molecular interactions inside cellular structures formed by memory proteins and her findings might lead to a better understanding of the relationship between normal brain function and disease. FACTS SAHIN’S PROJECT was one of the recipients of the Novo Nordisk Foundation’s postdoctoral fellowships 2019 for research abroad in the field of Bioscience and Basic Biomedicine. Cagla Sahin will receive DKK 3,640,073 over four years. What does this grant mean to you and your research? ”Thanks to the NNF grant, I get to spend three years at the Karolinska Institutet, Stockholm, where I will deepen my knowledge of mass spectrometry (MS), a really cool and advanced technique that enables the measurement of molecular weights, leading to insight of complex molecular assemblies. In particular I will use native MS and hydrogen-deuterium exchange MS to understand how molecular interactions and structural and conformational changes affect the function of amyloid-like proteins. This has never been done before, and I’m really looking forward to it! It is really exciting to get my own funding that supports my ideas and research, and gives me the opportunity to grow as a scientist this early in my career.” Where will you conduct your post-doc? ”The first three years I will be doing my postdoctoral research at the department of Microbiology, Tumor and Cell Biology at the Karolinska Institutet, in the group of Assistant Professor Michael Landreh and Professor Sir David Lane. Thereafter and for the last year of the project, I will join the group of Associate professor Kaare Teilum at the department of Biology at Copenhagen University, where another technique, nuclear magnetic resonance (NMR), will be used for structural characterization of amyloid-like proteins.” What applications could your research have? ”My research qualifies as basic science and focuses on expanding the knowledge of how the human memory is formed and stored. Specifically, I will investigate molecular interactions inside cellular structures formed by what are known as memory proteins, using native and hydrogendeuterium exchange MS. At the same time, studying such molecular interactions may lead to a better understanding of the molecular mechanisms involved in neurodegenerative diseases, such as Alzheimer’s and Parkinson’s and even cancer. Furthermore, this technique can be applied to understand molecular interactions in many other contexts, ranging from basic science to drug development and to protein formulation in industry.” What is the best thing about being a scientist and about your area of research? ”In general I love science and being a scientist. I like to develop new methods and protocols that can help shed light on a problem in a new way. Once you make any discovery – even tiny findings – they are a part of a bigger question, and I just find it thrilling and exciting to understand the everyday life – in nature, health and disease.” Do you have any advice for students out there wanting to pursue a career in science? ”If I were to give some general advice, one aspect would be to remember the life outside the science world, and really focus on finding that balance – it will make the road of the scientific career easier and more fun. Another piece of advice is to talk with the people in your network; supervisors, fellow-students, colleagues, nonscientist friends. Talking with others can open up your perspectives, whether it is regarding your career, for feedback on your development as a scientist/colleague/friend, or for a specific problem related to an experimental setup. Finally, find a good balance of optimism and realism. One will (most often) meet a lot of failure, before achieving that one positive result, which others might not even find as exciting as you do. Prepare your self by lowering your expectations, while striving for the best.” NLS TITLE: The superstructural biology of RNA-binding amyloid-like proteins in neurodegeneration and memory formation FACTS LIDDS Inside cells, proteins are busy fulfilling specific tasks by binding to other molecules, and wrong interactions can lead to disease. When the brain stores information, certain proteins selfassemble together with other molecules into large scaffolds that bind copies of different genes. These scaffolds resemble protein assemblies called “amyloid” that are a hallmark of diseases such as Alzheimer’s. Despite being LIDDS AB similar, one protein family forms functional, “good” structures, and the other pathogenic, “bad” ones. Sahin will use mass spectrometry, a technique that allows her to weigh proteins, and nuclear magnetic resonance spectroscopy that gives structural information, to follow their interactions to understand what makes protein assemblies in the brain bad or good. Which parts of the proteins bind together? Can we interfere with these interactions? Answering these questions will help us to better understand the relationship between normal brain function and disease. develops injectable drugs for cancer and other diseases based on a NanoZolid technology. NanoZolid helps solve some of the main problems with the way drugs work in the body and which affect patient quality of life. NanoZolid enables the controlled, long-term and personalized release of drugs for up to six months. NanoZolid can be combined with traditional small molecules, as well as with larger molecules. In March this year the United States Patent and Trademark Office issued a Notice of Allowance for the NanoZolid technology patent. The same patent was approved by the European Patent Office in 2018. With this new US patent, the NanoZolid technology will be protected until 2037 in both Europe and the US. NORDICLIFESCIENCE.ORG NORDICLIFESCIENCE.ORG 71 71