Клинов Дмитрий Владимирович

Кандидат физико-математических наук


Старший научный сотрудник (Лаборатория протеомики)

Тел.: +7 (495) 336-19-88

Эл. почта: klinov@ibch.ru

Избранные публикации

  1. Безуглов В.В., Грецкая Н.М., Клинов Д.В., Бобров М.Ю., Шибанова Е.Д., Акимов М.Г., Фомина-Агеева Е.В., Зинченко Г.Н., Баирамашвили Д.И., Мирошников А.И. (2009). Нанокомплексы рекомбинантных белков с полисиаловой кислотой. Получение, свойства и биологическая активность. Биоорг. хим. 35 (3), 350–356 ID:197
  2. Tuzikov A.B., Chinarev A.A., Gambaryan A.S., Oleinikov V.A., Klinov D.V., Matsko N.B., Kadykov V.A., Ermishov M.A., Demin I.V., Demin V.V., Rye P.D., Bovin N.V. (2003). Polyglycine II nanosheets: supramolecular antivirals? Chembiochem 4 (2-3), 147–54 [+]

    Tetraantennary peptides [glycine(n)-NHCH(2)](4)C can form stable noncovalent structures by self-assembly through intermolecular hydrogen bonding. The oligopeptide chains assemble as polyglycine II to yield submicron-sized, flat, one-molecule-thick sheets. Attachment of alpha-N-acetylneuraminic acid (Neu5Acalpha) to the terminal glycine residues gives rise to water-soluble assembled glycopeptides that are able to bind influenza virus multivalently and inhibit adhesion of the virus to cells 10(3)-fold more effectively than a monomeric glycoside of Neu5Acalpha. Another antiviral strategy based on virus-promoted assembly of the glycopeptides was also demonstrated. Consequently, the self-assembly principle offers new perspectives on the design of multivalent antivirals.

    ID:36