An investigation of the ionophoric characteristics of destruxin A

Destruxin A, a cyclohexadepsipeptide related to the enniatins and beauvericin, exhibits ionophoric properties. Calcium ion mobilization across liposomal membrane barriers, for example, has been demonstrated using the calcium ion-sensitive dyes Arsenazo III and Fura-2. Initial molecular mechanics/mol...

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Bibliographic Details
Published in:Archives of biochemistry and biophysics 2002-09, Vol.405 (1), p.73-77
Main Authors: Hinaje, Maria, Ford, Martyn, Banting, Lee, Arkle, Steve, Khambay, Bhupinder
Format: Article
Language:English
Subjects:
Calcium
Calcium - metabolism
Cations
Chelating Agents - pharmacology
Depsipeptides
Destruxin
Ionophore
Ionophores - pharmacology
Ions
Liposomes
Liposomes - metabolism
Models, Chemical
Models, Molecular
Molecular modeling
Peptides, Cyclic - pharmacology
Software
Time Factors
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Summary:Destruxin A, a cyclohexadepsipeptide related to the enniatins and beauvericin, exhibits ionophoric properties. Calcium ion mobilization across liposomal membrane barriers, for example, has been demonstrated using the calcium ion-sensitive dyes Arsenazo III and Fura-2. Initial molecular mechanics/molecular dynamics calculations indicate the potential for destruxin A to form a coordination complex with calcium in which the divalent cation is bound at the center of a sandwich formed by two molecules of destruxin A. This novel calcium ion binding may help explain the diverse biological effects exhibited by the destruxins.
ISSN:0003-9861
1096-0384
DOI:10.1016/S0003-9861(02)00275-8