In the past decade substantial progress has been made in understanding the organization and biological activity of amphotericin B (AmB) in the presence of sterols in lipid environments. This review concentrates mainly on interactions of AmB with lipids and sterols, AmB channel formation in membranes, AmB aggregation, AmB modifications important for understanding its biological activity, and AmB models explaining its mechanism of action. Most of the reviewed studies concern monolayers at the water–gas interface, monolayers deposited on a solid substrate by use of the Langmuir–Blodgett technique, micelles, vesicles, and multi-bilayers. Liposomal AmB formulations and drug delivery are intentionally omitted, because several reviews dedicated to this subject are already available.

The interface of Cu͑001͒ electrode surfaces in 10 mM HCl solution was studied by in situ surface x-ray diffraction and density functional theory, focusing on the precise structure of the c͑2 ϫ 2͒ Cl adlayer formed at positive potentials. Crystal truncation rod measurements in this adsorbate phase at a potential of −0.20 V Ag/AgCl reveal distinct differences to corresponding data by Tolentino et al. ͓Surf. Sci. 601, 2962 ͑2007͔͒ for the c͑2 ϫ 2͒ Cl structure formed at the Cu͑001͒-vacuum interface. Although in both environments, the atoms in the second Cu layer exhibit a small vertical corrugation, the sign of this corrugation is reversed. Furthermore, also the Cu-Cl bond distance and the average Cu interlayer spacings at the surface differ. Ab initio calculations performed for this adsorbate system reproduce these effects-specifically the reversal of the subsurface second-layer buckling caused in the presence of coadsorbed water molecules and cations in the outer part of the electrochemical double layer. In addition, studies at more negative potentials reveal a continuous surface phase transition to a disordered Cl adlayer at −0.62 V Ag/AgCl , but indicate a substantial Cl coverage even at the onset of hydrogen evolution.

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