LOCATION OF A LAMININ PEPTIDE FRAGMENT IN PHOSPHOLIPID MONO AND BILAYERS

The surface properties of a laminin related decapeptide were determine d using Langmuir films. Moreover, its interaction with phospholipids w as studied using both DPPC mono- and bi-layer liposomes as membrane mo dels. Changes in fluidity of the bilayers induced by this peptide were determined by means of polarizable probes such as 8-anilino-1-naphtha lene sulfonic acid (ANS) and 1,3,5-diphenylhexatriene (DPH). Changes i n permeability of liposomes were studied through CF latency. The resul ts of surface properties and liposome interactions suggest that this p eptide forms some type of aggregate in water solution that competes wi th its incorporation at a water-air interface and with its binding to bilayers. (C) 1998 Elsevier Science B.V. All rights reserved.