It is well known the high affinity of clotrimazole for the haeme moiety. I wander whether its binding to haemoglobin has been studied and if it depends on the oxido-reduction state of the Fe atom. I would greatly appreciate any comment.
Eventually Met-Hb may interact with clotrimazol as colleagues from India state :http://www.eurekaselect.com/106601/article. I have never come across the comparison of kinetics or thermodynamics of CLZ interaction with reduced or oxidized Hb. The authors of the paper may know more about it...
As we pointed out in our paper in AJPCELL in 2008, clotrimazole interacts with P450 proteins, hence with heme group containing molecules, like hemoglobin. We do not know the role of P450 in the regulation of IK channels. It would be interesting to use hemoglobin as a simpler accessible molecule and study its interaction with the heme group as function of its oxidation state.
From Page C830 of AJPCell 294, 2008:
Neither typical inhibitors of Big conductance (BK), other
voltage-gated K channels, Small conductance (SK) channels,
nor known blockers of the connexin family were effective
(Table 2) (15). Only CTZ with an approximate IC50 of 25 M
and completely at 50 M prevented Kc loss (Fig. 10). This
concentration range is comparable to published CTZ doses in
other epithelial cell systems, with intermediate conductance
KCa3.1 (IK) channels involved in RVD (29, 60). TRAM-34, an
inhibitor of IK channels not involving the P450 protein like
CTZ (56, 66), also reduced Kc loss by 50% and less Rb influx
suggesting that the two inhibitors act through different mechanism
either at the channel or regulatory level.
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