Kissper is a 39-residue peptide isolated from kiwi fruit (Actinidia deliciosa). It derives from the processing of kiwellin, a well-represented novel allergenic protein found in the edible part of the fruit (Tamburrini et al., 2005, Protein J. 24, 423–9). In fact, its primary structure is identical to the N-terminal region of kiwellin. Kissper has six cysteine residues forming three disulfide bridges. In a previous study, we demonstrated that kissper forms pores with channel-like activity. The aim of this study was to monitor the kissper channel current in lipid bilayer membranes made up of DOPS:DOPE:POPC (27:27:18, w:w:w), a surrogate of intestinal membrane, in different salt solutions, i.e. KCl, potassium gluconate and potassium citrate (1 M, pH=7.0). A voltage-clamp technique was used. The results of this study indicate that a) kissper forms ion channels in DOPS:DOPE:POPC PLMs in all salt solutions used, b) the mean conductance (Lc) and occurrence (n° events/min) values depend on applied voltages, and c) in asymmetric salt solutions, kissper-permeabilized membrane shifts the selectivity towards either anions or cations, depending on the nature of the salts used. Recent studies suggest that many bioactive molecules from plant source may have beneficial effects on human health beyond their nutritional properties. The capacity of kissper to form channel-like pathways in a lipid bilayer, whose composition is similar to that found in intestinal cells, suggests potential biological effects on human health.