ABSTRACT
Bacteriocin AS-48 produced by Enterococcus faecalis S-48 is a ribosomally synthesized cyclic peptide (7.4 kDa) of broad inhibitory spectrum against Gram-positive and Gram-negative bacteria. Simple monolayers of AS-48 and of dipalmitoyl phosphatidic acid (DPPA) at the air-water interface are studied. The AS-48 interfacial behavior in the function of pH explains the biological activity of the peptide. The lipid monolayers show the characteristic behavior of phosphatidic acid at the mentioned interface. The interactions between AS-48 and DPPA, a majority lipid of the bacterial cell membrane, are quantitatively investigated. The results indicate that only when the lipid molecules are charged enough (pH 10.5) is an attractive interaction between AS-48 and DPPA observed, although under these experimental conditions the results seem to indicate that a deformation of the peptide helical structure could take place. Copyright 2001 Academic Press.
