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Carborane‐Based Analogues of 5‐Lipoxygenase Inhibitors Co‐inhibit Heat Shock Protein 90 in HCT116 Cells
Author(s) -
Kuhnert Robert,
Sárosi MenyhártBotond,
George Sven,
Lönnecke Peter,
Hofmann Bettina,
Steinhilber Dieter,
Steinmann Sara,
SchneiderStock Regine,
Murganić Blagoje,
Mijatović Sanja,
MaksimovićIvanić Danijela,
HeyHawkins Evamarie
Publication year - 2019
Publication title -
chemmedchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201800651
Subject(s) - lipoxygenase , chemistry , heat shock protein , arachidonate 5 lipoxygenase , cytotoxicity , arachidonic acid , cell culture , angiogenesis , biochemistry , enzyme , cancer research , biology , in vitro , genetics , gene
5‐Lipoxygenase converts arachidonic acid into leukotrienes, which are involved in inflammation and angiogenesis. The introduction of carboranes can improve the pharmacokinetic behavior of metabolically less stable pharmaceutics. Herein we report the syntheses of several carborane‐based inhibitors of the 5‐lipoxygenase pathway. The isosteric replacement of phenyl rings by carboranes leads to improved cytotoxicity toward several melanoma and colon cancer cell lines. For the colon cancer cell line HCT116, the co‐inhibition of heat shock protein 90 was observed.