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Sensitized photomodification of oligonucleotide-binding proteins displayed on the eucaryotic cell surface

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Abstract

Interactions of double-stranded nucleic acids with cell surface proteins, which are involved in binding and transport of extracellular nucleic acids, were studied by the photoaffinity modification with a binary system of oligonucleotide conjugates. The photoreactive double-stranded complex involved an oligonucleotide template and two complementary to adjacent sequences oligonucleotide conjugates. One conjugate contained a photoreagent, viz., 4-azido-2,3,5,6-tetrafluorobenzaldehyde N-(3-aminopropionyl)hydrazone, at the terminus located in proximity to the terminus of another conjugate containing the sensitizer, viz., 9-aminomethylanthracene. Binding of photoreagent and the sensitizer to a single-stranded template yields the photoreactive center. Upon irradiation with visible light (400—580 nm), this photoreactive double-stranded complex forms covalent cross-linkages with oligonucleotide-binding surface proteins of eucaryotic SPEV cells.

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Authors and Affiliations

  1. Novosibirsk Institute of Bioorganic Chemistry, 8 prosp. Akad. Lavrent"eva, 630090, Novosibirsk, Russian Federation

    T. I. Gainutdinov, O. E. Shestova, L. A. Yakubov, M. I. Dobrikov & V. V. Vlassov

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  1. T. I. Gainutdinov
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  2. O. E. Shestova
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  3. L. A. Yakubov
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  4. M. I. Dobrikov
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  5. V. V. Vlassov
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Gainutdinov, T.I., Shestova, O.E., Yakubov, L.A. et al. Sensitized photomodification of oligonucleotide-binding proteins displayed on the eucaryotic cell surface. Russian Chemical Bulletin 51, 1198–1203 (2002). https://doi.org/10.1023/A:1020940210953

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