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Benzylisoquinoline compounds inhibit the ability of calmodulin to activate cyclic nucleotide phosphodiesterase.

Benzylisoquinoline compounds antagonised the ability of calmodulin ( CaM) to stimulate the activity of calmodulin-dependent cyclic nucleotide phosphodiesterase (CaM-PDE). This 'anti- CaM' activity was related to the hydrophobicity of the non-polar terminal region of the antagonist molecule. Antagonistic potency increased with the increase of hydrophobicity; the anti- CaM activity did not change when the polar terminus was a tertiary amine or quarternary amine. The anti- CaM potency was greater for bisbenzylisoquinoline compounds than for monobenzylisoquinoline compounds. Among the bisbenzylisoquinoline compounds anti- CaM pathway was: D3 greater than D2 berbamine greater than daurisoline greater than dauricine. Compound D3, which exhibited an IC50 value of 2.8 microM, was one of the most potent calmodulin antagonists, among benzylisoquinoline compounds, so far reported.[1]

References

  1. Benzylisoquinoline compounds inhibit the ability of calmodulin to activate cyclic nucleotide phosphodiesterase. Hu, Z.Y., Chen, S.L., Hao, Z.G., Huang, W.L., Peng, S.X. Cell. Signal. (1989) [Pubmed]
 
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