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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
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...
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Published in: | Journal of medicinal chemistry 2012-06, Vol.55 (11), p.5529-5535 |
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Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | 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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ISSN: | 0022-2623 1520-4804 |
DOI: | 10.1021/jm3004587 |