Protein molecules act as mini antennas in cells
Researchers led by Josef Lazar from the Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences (IOCB Prague) have shown that molecules of fluorescent proteins act as antennas with optical properties (i.e. the ability to absorb and emit light) in Depending on their space, orientation work. Fluorescent proteins, first discovered in jellyfish, are now widely used in studies of molecular processes in living cells and organisms. The newly described properties of these molecules will be used both in basic biological research and in novel drug research. A team of researchers from the IOCB Prague, the Institute of Microbiology and the Institute of Molecular Genetics of the Czech Academy of Sciences published their results in the journal Proceedings of the National Academy of Sciences of the United States of America.
To achieve these results, the researchers produced sufficient quantities of fluorescent proteins using genetically modified bacteria, identified the conditions under which the proteins form crystals, and determined the atomic structure of the crystals. Using a unique microscope that was developed within the group, they then measured how these crystals absorb and emit light and calculated the directional properties of the individual molecules from the data. In this way, they were able to check whether the fluorescent protein molecules do not behave as tiny luminescence points, as they are often wrongly assumed, but as miniature antennas. Similar to antennas for radio, WiFi and television transmission, these molecules only absorb light from certain directions. They also only emit light in certain directions. The researchers also managed to pinpoint these directions.
The possibility that fluorescent protein molecules behave as antennas capable of absorbing extraneous light has been suggested, but it has long proven difficult to confirm, and this limited its applications. The obstacles were overcome by Josef Lazar from IOCB Prague and his team, which specializes in the development and application of advanced optical microscopy methods.
“Based on the results of others and our own laboratories, we hypothesized that fluorescent protein molecules likely act as antennas. Still, we were surprised to see how true this analogy is and how accurately we could determine the directions from which these molecules absorb light and emit, “says Josef Lazar.
The fact that fluorescent protein molecules act as miniature antennas is not only interesting out of curiosity of physics, but can also have important practical applications. Attaching a fluorescent protein to another protein of interest means attaching a miniature antenna to it which can then be used to detail changes in the shape of the molecules of the protein of interest directly in a living cell. Such changes in the molecular shape can be induced, for example, by a drug. The present discovery will therefore find application in the study of important physiological processes at the molecular level as well as in the discovery of new drugs.
“The significance of our finding lies in the fact that fluorescent protein molecules, although widely used in biological research, have not yet been fully assessed and also not really exploited their ability to behave like antennas. Knowledge of the directional properties of fluorescent proteins can lead to new ways of using these useful molecules, “explains Lazar.
In cooperation with other groups at the IOCB Prague, Josef Lazar’s team is already trying to apply the available findings, for example, to the study of the physiological effects of insulin and the development of insulin substitutes for oral use. Another example of a possible application of the present discovery is in tracking electrical signals in nerve cells that could be useful in studying the brain and neurological disorders.
Reference: Myšková J., Rybakova O., Brynda J., Khoroshyy P., Bondar A., Lazar J. Directionality of light absorption and emission in representative fluorescent proteins. PNAS 2020. doi: 10.1073 / pnas.2017379117
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