Compact Conformation of Ba(2+)-Beauvericin Complex by Triple Cation-π Interactions: Insight into Ion Transport Mechanism from Gas-Phase Structures

通过三重阳离子-π相互作用形成Ba(2+)-博维菌素复合物的紧凑构象:从气相结构深入了解离子传输机制

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Abstract

Beauvericin (BEA), a natural cyclic hexadepsipeptide ionophore, can selectively transport metal ions through lipid bilayers. Although BEA can transport Ca(2+) and Ba(2+), previous studies have not yet revealed its ion-selective transport mechanism. In the present study, we identified a novel conformation of 1:1 BEA complexes selectively stabilized by triple cation-π interactions with Ba(2+) among alkaline-earth and alkali metal ions, using electrospray ionization-ion mobility-mass spectrometry (ESI-IM-MS). The calculated IR spectrum of this conformation was well reproduced with the experimental IR photodissociation spectrum of the 1:1 BEA complex with Ba(2+), which was not assigned previously. This conformation can maximize membrane permeability across lipid bilayers since its size (collision cross section) and polarity (solvent accessible 3D polar surface area) are very small and apolar, respectively. The gas phase structures provide insight into BEA's structure-function relationship, in which the formation of a compact and apolar conformation facilitates ion-selective transport.

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