A potent and highly selective inhibitor of human α-1,3-fucosyltransferase via click chemistry

Lac V. Lee, Michael L. Mitchell, Shih Jung Huang, Valery V. Fokin, K. Barry Sharpless, Chi Huey Wong

Результат исследований: Материалы для журналаСтатьярецензирование

432 Цитирования (Scopus)

Аннотация

Potent inhibitors of fucosyltransferases, and glycosyltransferases in general, have been elusive due to the inherent barriers surrounding the family of glycosyltransfer reactions. The problems of weak substrate affinity and low catalytic proficiency of fucosyltransferase was offset by recruiting additional binding features, in this case hydrophobic interactions, to produce a high affinity inhibitor, 24, with Ki = 62 nM. The molecule was identified from a GDP-triazole library of 85 compounds, which was produced by the Cu(I)-catalyzed [2 + 3] cycloaddition reaction between azide and acetylene reactants, followed by in situ screening without product isolation.

Язык оригиналаАнглийский
Страницы (с-по)9588-9589
Число страниц2
ЖурналJournal of the American Chemical Society
Том125
Номер выпуска32
DOI
СостояниеОпубликовано - 13 авг 2003
Опубликовано для внешнего пользованияДа

ASJC Scopus subject areas

  • Chemistry(all)

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