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Hindawi, BioMed Research International, (2014), p. 1-9, 2014

DOI: 10.1155/2014/389869

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Carborane-Based Carbonic Anhydrase Inhibitors: Insight into CAII/CAIX Specificity from a High-Resolution Crystal Structure, Modeling, and Quantum Chemical Calculations

Journal article published in 2014 by Pavl Xed Na X. Ez Xe X. D. Ov Xe, Pavel Mader ORCID, Adam Pecina, Petr Cígler, Petr C. Xed Gler, Bohum Xed R. Gr Xfc Ner, Martin Lepšík, Václav Šícha, Vaclav Sicha, Pavel Hobza, V. Xe Clav X. Xed Cha, Bohumír Grüner, Ji X. Xed Brynda, Jindřich Fanfrlík, Jiří Brynda and other authors.
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Carborane-based compounds are promising lead structures for development of inhibitors of carbonic anhydrases (CAs). Here, we report structural and computational analysis applicable to structure-based design of carborane compounds with selectivity toward the cancer-specific CAIX isoenzyme. We determined the crystal structure of CAII in complex with 1-methylenesulfamide-1,2-dicarba-closo-dodecaborane at 1.0 Å resolution and used this structure to model the 1-methylenesulfamide-1,2-dicarba-closo-dodecaborane interactions with CAIX. A virtual glycine scan revealed the contributions of individual residues to the energy of binding of 1-methylenesulfamide-1,2-dicarba-closo-dodecaborane to CAII and CAIX, respectively.