| Literature DB >> 31568723 |
Bohumír Grüner1, Jiří Brynda2,3, Viswanath Das4,5, Václav Šícha1, Jana Štěpánková4,5, Jan Nekvinda1,6, Josef Holub1, Klára Pospíšilová2, Milan Fábry3, Petr Pachl2, Vlastimil Král3, Michael Kugler2, Vlastimil Mašek4, Martina Medvedíková4, Stanislava Matějková2, Alice Nová4, Barbora Lišková4, Soňa Gurská4, Petr Džubák4,5, Marián Hajdúch4,5, Pavlína Řezáčová2,3.
Abstract
Carbonic anhydrase IX (CAIX) is a transmembrane enzyme that regulates pH in hypoxic tumors and promotes tumor cell survival. Its expression is associated with the occurrence of metastases and poor prognosis. Here, we present nine derivatives of the cobalt bis(dicarbollide)(1-) anion substituted at the boron or carbon sites by alkysulfamide group(s) as highly specific and selective inhibitors of CAIX. Interactions of these compounds with the active site of CAIX were explored on the atomic level using protein crystallography. Two selected derivatives display subnanomolar or picomolar inhibition constants and high selectivity for the tumor-specific CAIX over cytosolic isoform CAII. Both derivatives had a time-dependent effect on the growth of multicellular spheroids of HT-29 and HCT116 colorectal cancer cells, facilitated penetration and/or accumulation of doxorubicin into spheroids, and displayed low toxicity and showed promising pharmacokinetics and a significant inhibitory effect on tumor growth in syngenic breast 4T1 and colorectal HT-29 cancer xenotransplants.Entities:
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Year: 2019 PMID: 31568723 DOI: 10.1021/acs.jmedchem.9b00945
Source DB: PubMed Journal: J Med Chem ISSN: 0022-2623 Impact factor: 7.446