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Siberian scientists suggest using fluorescent proteins to analyze toxicity

The results of the study might help in creating a new type of pharmaceuticals

MOSCOW, July 26. /TASS/. Researchers from the Institute of Biophysics at Siberian Branch of Russian Academy of Science and Siberian Federal University (SFU) investigated the influence of toxins on fluorescent proteins. The results of the study might help in creating a new type of pharmaceuticals, the SFU press office said.

For research objects, fluorescent proteins containing marine organisms, for example, the sea nettles Aequorea and Phialidium (Clytia) and hydropolip Obelia longissima, were chosen. The proteins of these organisms contain coelenterazine, an organic substance which upon oxidation is transformed into coelenteramide which in turn can emit luminescence when kindled by the light.

"By using fluorescent coelenteramide-containing proteins, we move the understanding of toxicity effects to the level of elementary physical and chemical processes. Perhaps, this direction will lead to the development of new types of medicines and to rethinking the already described effects," the study’s co-author, Doctor of Physical and Mathematical Sciences, Professor at the Chair of SFU’s Physical and Inorganic Chemistry of School of Non-Ferrous Metals and Materials Science Nadezhda Kudryashova commented.

Researchers exposed coelenteramide to temperature, poisonous substances (e.g. alcohol), and beta and gamma radiation. They found out that under the influence of all these factors, the fluorescent protein changes its color from blue-green to purple. According to the scientists, the toxicity of the surrounding media can be evaluated by "changes in the contribution of purple and blue-green": the more purple light protein emits, the stronger the toxicity of the media is.

Scientists also managed to clarify how adverse factors influence the protein on the molecular level. The molecule of coelenteramide is photochemically active: kindled by the light, it can donate a proton by turning from neutral to ionized form. Every distortion of the molecule’s structure as a result of external factors (chemical, radiational, thermal) leads to a decrease in the proton transfer’s efficiency and to the increase of purple fluorescence emitted.

The luminescent analysis is widely used in medicine and biology. However, the authors of study presume that the prospects of using coelenteramide-containing proteins are overlooked by the research community. The current research work is aimed at filling this gap.