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Previously, we have reported that spherical particles (SPs) are formed by the thermal remodeling of rigid helical virions of native tobacco mosaic virus (TMV) at 94°C. SPs have remarkable features: stability, unique adsorption properties and immunostimulation potential. Here we performed a comparative study of the amino acid composition of the SPs and virions surface to characterize their properties and take an important step to understanding the structure of SPs. The results of tritium planigraphy showed that thermal transformation of TMV leads to a significant increase in tritium label incorporation into the following sites of SPs protein: 41–71 а.a. and 93–122 a.a. At the same time, there was a decrease in tritium label incorporation into the N- and C- terminal region (1–15 a.a., 142–158 a.a). The use of complementary physico-chemical methods allowed us to carry out a detailed structural analysis of the surface and to determine the most likely surface areas of SPs. The obtained data make it possible to consider viral protein thermal rearrangements, and to open new opportunities for biologically active complex design using information about SPs surface amino acid composition and methods of non-specific adsorption and bioconjugation.

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Comparison of ion-molecular reactions of free-phenyl cations generated by tritium β-decay with 2-methyl- and 2-phenylquinolines has been investigated. The reaction of direct nitrogen atom phenylation with the help of nucleogenic phenyl cations has been fulfilled for the first time and a new one-step synthesis of tritium-labeled N-phenyl-2-phenylquinolinium salt—lipophilic radioactive biological marker has been elaborated.