Присоединение тривалина изменяет специфичность связывания аналога нетропсина с ДНК

Лейнсоо, Т.А.; Николаев, В.А.; Гроховский, С.Л.; Стрельцов, С.А.; Заседателев, А.С.; Жузе, А.Л.; Гурский, Г.В.

Авторы: Лейнсоо Т.А., Николаев В.А., Гроховский С.Л., Стрельцов С.А., Заседателев А.С., Жузе А.Л., Гурский Г.В.
Журнал: Молекулярная биология
Том: 22
Номер: 1
Год издания: 1988
Первая страница: 159
Последняя страница: 175
Аннотация: The interaction with DNA is discussed for three analogs of the antibiotic netropsin, each of which contains two N-propylpyrrolecarboxamide fragments, to which Dns-Gly-Val-Val-Val-Gly-Gly (analog I), Val-Val-Val-Gly-Gly (analog II), and Gly- Gly- (analog III) are covalently bonded. It is shown that analogs I and II form associates in aqueous solution and methanol, which is manifested in the concentration dependence of the shape of the absorption and circular dichroism spectra. In contrast to the analogs I and II, analog III is in monomer form up to a concentration of ~1•10-3 M. A determination of the apparent size of the intermolecular associates by gel filtration showed that analog I at a concentration of 1• 10-3 M forms associates consisting of 2-12 monomers. Analog II is less inclined to form high-order associates than analog I. The dimerization constants were determined for analogs I and II in aqueous solution and methanol. Interaction of the N-propylpyrrolecarboxamide and peptide fragments with DNA was recorded for analog I independently by circular dichroism and fluorescent methods. If the analog I (or II) was in an autoassociated form in solution, then the specificity of its binding to different nucleotide sequences differed appreciably from the specificity of the binding of analog III. The results of our experiments agree with the hypothesis that analogs I and II in the /3-associated form recognize base pair sequences in which two sites, consisting of three AT pairs in a row, are separated by two GC pairs.
Добавил в систему: Гурский Георгий Валерианович

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Присоединение тривалина изменяет специфичность связывания аналога нетропсина с ДНКстатья

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