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@ARTICLE{Dudutien:205428,
author = {Dudutienė, Virginija and Matulienė, Jurgita and Smirnov,
Alexey and Timm, David D. and Zubrienė, Asta and
Baranauskienė, Lina and Morku̅naitė, Vaida and
Smirnovienė, Joana and Michailovienė, Vilma and
Juozapaitienė, Vaida and Mickevičiu̅tė, Aurelija and
Kazokaitė, Justina and Bakšytė, Sandra and
Kasiliauskaitė, Aistė and Jachno, Jelena and Revuckienė,
Jurgita and Kišonaitė, Miglė and Pilipuitytė, Vilma and
Ivanauskaitė, Eglė and Milinavičiu̅tė, Goda and
Smirnovas, Vytautas and Petrikaitė, Vilma and Kairys,
Visvaldas and Petrauskas, Vytautas and Norvaišas, Povilas
and Lingė, Darius and Gibieža, Paulius and Čapkauskaitė,
Edita and Zakšauskas, Audrius and Kazlauskas, Egidijus and
Manakova, Elena and Gražulis, Saulius and Ladbury, John E.
and Matulis, Daumantas},
title = {{D}iscovery and {C}haracterization of {N}ovel {S}elective
{I}nhibitors of {C}arbonic {A}nhydrase {IX}},
journal = {Journal of medicinal chemistry},
volume = {57},
number = {22},
issn = {1520-4804},
address = {Washington, DC},
publisher = {ACS},
reportid = {PUBDB-2015-00005},
pages = {9435 - 9446},
year = {2014},
note = {(c) American Chemical Society. Post referee full text in
progress. Embargo for full text 1 year from October 30,
2014.},
abstract = {Human carbonic anhydrase IX (CA IX) is highly expressedin
tumor tissues, and its selective inhibition provides a
potential target forthe treatment of numerous cancers.
Development of potent, highlyselective inhibitors against
this target remains an unmet need in anticancertherapeutics.
A series of fluorinated benzenesulfonamides with
sub-stituents on the benzene ring was designed and
synthesized. Several ofthese exhibited a highly potent and
selective inhibition profile against CAIX. Three fluorine
atoms significantly increased the affinity by withdrawing
electrons and lowering the pKa of thebenzenesulfonamide
group. The bulky ortho substituents, such as cyclooctyl or
even cyclododecyl groups, fit into thehydrophobic pocket in
the active site of CA IX but not CA II, as shown by the
compound’s co-crystal structure with chimeric CAIX. The
strongest inhibitor of recombinant human CA IX’s catalytic
domain in human cells achieved an affinity of 50 pM.However,
the high affinity diminished the selectivity. The most
selective compound for CA IX exhibited 10 nM affinity.
Thecompound that showed the best balance between affinity
and selectivity bound with 1 nM affinity. The inhibitors
described inthis work provide the basis for novel anticancer
therapeutics targeting CA IX.},
cin = {EMBL-User},
ddc = {540},
cid = {I:(DE-H253)EMBL-User-20120814},
pnm = {PETRA Beamline P13 (POF2-54G14) / PETRA Beamline P14
(POF2-54G14)},
pid = {G:(DE-H253)POF2-P13-20130405 /
G:(DE-H253)POF2-P14-20130405},
experiment = {EXP:(DE-H253)P-P13-20150101 / EXP:(DE-H253)P-P14-20150101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000345722200015},
pubmed = {pmid:25358084},
doi = {10.1021/jm501003k},
url = {https://bib-pubdb1.desy.de/record/205428},
}