Abstract:
:The mechanism by which diverse drugs modulate voltage-dependent Ca2+ channels is ill-understood. We have approached this problem by examining the interaction of verapamil with a 97-residue synthetic channel peptide (SCP) that exhibits functional similarities to authentic L-type Ca2+ channels in terms of cation selectivity and permeation as well as interaction with channel-activating and blocking drugs (Grove et al. (1991) Proc. Natl. Acad. Sci. USA 88, 6418). Different possibilities of binding of verapamil inside the Ca(2+)-bound SCP were simulated using the Monte Carlo-with-energy-minimization method. In the optimal mode of the binding, verapamil adopted a folded conformation and fit snugly in the pore. The dimethoxyphenyl groups of the drug interacted with two Ca2+ ions coordinated to the acidic residues of SCP, thus forming a ternary complex of the drug, Ca2+, and channel. The isopropyl group of verapamil abetted a ring of four Ile residues constituting the putative SCP gate. The occlusion of this gate by verapamil in this manner was strikingly similar to that accomplished by the methyl group of dihydropyridine drugs. In conjunction with an earlier study on SCP bound to dihydropyridine drugs (Zhorov and Ananthanarayanan (1996) Biophys. J. 70, 22), our data suggest that, in general, drug modulation of SCP would involve the interaction of the ligands with the pore-bound Ca2+ and with the hydrophobic gate. In light of the functional similarity between SCP and L-type Ca2+ channel, it is likely that the latter would also interact with drugs in a similar fashion.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Zhorov BS,Ananthanarayanan VSdoi
10.1006/abbi.1997.9968subject
Has Abstractpub_date
1997-05-15 00:00:00pages
238-44issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(97)99968-9journal_volume
341pub_type
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