Colistin is an antibiotic member of the polymixin family, showing a hi
gh amphipathic character. Its mechanism of action has been related to
its ability to disrupt phospholipid bilayers of the bacterial membrane
. Due to its hydrophobic properties colistin can interact both with th
e polar heads and the alkyl chains of the phospholipids. Moreover, it
has a polycationic structure, so its interactions with phospholipids s
hould be highly dependent on the electric charge of the lipid and the
ionisation state of polymixin molecule. In the present paper we report
on physicochemical studies to define the type and characteristics of
these interactions. The surface activity of colistin has been shown to
be highly dependent on the pH of the medium, the less protonated form
s being more stable at the air-water interface. Interaction with phosp
holipid monolayers shows the same tendency. Colistin is also able to f
orm mixed monolayers with phospholipids with small deviations from ide
ality. Physicochemical studies carried out with fluorescent probes ind
icate the presence of pure colistin aggregates that can coexist with m
ixed micelles composed of colistin/phospholipids. In no case did the i
nteraction cause significative changes in the transition temperature o
f phospholipids. (C) 1998 Elsevier Science B.V.