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Protein-protein interactions: Inhibition of mammalian carbonic anhydrases I-XV by the murine inhibitor of carbonic anhydrase and other members of the transferrin family

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Details

Original languageEnglish
Pages (from-to)5529-5535
Number of pages7
JournalJOURNAL OF MEDICINAL CHEMISTRY
Volume55
Issue number11
DOIs
Publication statusPublished - 14 Jun 2012
Publication typeA1 Journal article-refereed

Abstract

The murine inhibitor of carbonic anhydrase (mICA), a member of the transferrin (TF) superfamily of proteins, together with human holo- and apoTF and lactoferrin (LF) were assessed as inhibitors of all catalytically active mammalian (h = human, m = murine) CA isoforms, from CA I to CA XV. mICA was a low nanomolar to subnanomolar inhibitor of hCAs I, II, III, VA, VB, VII and mCAs XV (K I of 0.7-44.0 nM) and inhibited the remaining isoforms with K I of 185.5-469 nM. hTF, apoTF, and hLF were inhibitors of most of these CAs but with reduced efficiency compared to mICA (K I of 18.9-453.8 nM). Biacore surface plasmon resonance and differential scanning calorimetry experiments were also used for obtaining more insights into the interaction between these proteins, which may be useful for drug design of protein-based CA inhibitors.

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