The distance measured is in the nanometer range (one millionth of a millimeter). This technique is called ''electron paramagnetic resonance spectroscopy'' (EPR) or ''electron spin resonance''. ''When two nanobodies bind to the transporter, we can measure the distance between the two magnetic probes in cells using our EPR methods'', explains Enrica Bordignon. The multidisciplinary team also included scientists from the Ruhr University Bochum (cluster of excellence RESOLV) and the University of Osnabrueck, Germany, and the University of Southampton, UK.īeforehand, a small magnetic probe (a molecule carrying unpaired electrons) was attached to each nanobody. coli cells, two nanobodies target the desired membrane protein on the inner membrane of the cell and attach to it,'' explains Markus A. The scientists have thus artificially produced specific nanobodies for a membrane transporter and use them to directly report on its structure. ''These are fragments of antibodies that are able to recognise and bind to a specific target, such as an antigen or in our case, a membrane transporter, in a very efficient way,'' explains Enrica Bordignon. To achieve this, the research team relied on a specific ''tool'': nanobodies. Seeger, associate professor at the Institute for Medical Microbiology at the UZH, has developed a new method for studying membrane proteins in action in living cells more precisely, in the inner cell membranes of the intestinal bacterium E. Proteins outside their native environment might show different structural properties, therefore misleading drug development.Ī team led by Enrica Bordignon, full professor in the Department of Physical Chemistry at the UNIGE Faculty of Science, in collaboration with Markus A. In any case, these strategies remove them from their physiological environment and do not allow their functioning to be finely observed in situ. They can also be inserted into artificial membranes called ''nanodiscs'', made of proteins and lipids, or in pure lipidic membranes. They must be maintained in liquid solutions composed of detergents. Once extracted, membrane proteins cannot be studied in aqueous solutions. To characterize them, scientists must extract these proteins from the cell membrane in which they are found and isolate them from all other proteins. The biophysical study of their structure - the spatial organization of the constituent amino acids - is therefore essential. As a result, membrane proteins represent more than 60% of current drug targets. in the communication system of cells that allows them to coordinate their metabolic processes, development and organisation. Located at the interface between the outside and inside of the cell, they carry various substances across the membrane - into or out of the cell - and play a crucial role in cell signaling, i.e. The proteins attached to this membrane are called ''membrane proteins''. It separates the contents of the cell from its direct environment and regulates the substances that can enter or leave the cell. This membrane consists of a double layer of lipids. In living organisms, each cell is surrounded by a cell membrane (or ''cytoplasmic membrane'').
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