An investigation of the ionophoric characteristics of destruxin A

M. Hinaje; M. Ford; Lee Banting; Stephen Arkle; B. Khambay

doi:10.1016/S0003-9861(02)00275-8

An investigation of the ionophoric characteristics of destruxin A

M. Hinaje, M. Ford, Lee Banting, Stephen Arkle, B. Khambay

School of Pharmacy & Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

Abstract

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.

Original language	English
Pages (from-to)	73-77
Number of pages	5
Journal	Archives of Biochemistry and Biophysics
Volume	405
Issue number	1
DOIs	https://doi.org/10.1016/S0003-9861(02)00275-8
Publication status	Published - 1 Sept 2002

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abstract = "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.",

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AU - Arkle, Stephen

AU - Khambay, B.

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AB - 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.

U2 - 10.1016/S0003-9861(02)00275-8

DO - 10.1016/S0003-9861(02)00275-8

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JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

IS - 1

ER -

An investigation of the ionophoric characteristics of destruxin A

Abstract

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