Fluorescence microscopy of Langmuir films is used to determine the effect o
f polyphosphoinositides (PPIs) on the structure of phosphatidylcholine-cont
aining monolayers. Dramatic alterations in the texture of these films occur
as the fraction of PPI in the film is altered. These changes depend on the
ionic strength of the underlying subphase and can be accounted for by cons
idering the electrostatic interactions among PPIs. Surface adsorption of a
fluorescent peptide derivative based on the PPI binding site of the protein
gelsolin co-localizes with PPI-rich domains. Localization of polyphosphoin
ositides in domains within the inner leaflet of the plasma membrane is prop
osed to be a key element in some aspects of intracellular signaling, and th
ese data have implications for explaining the cause of restructuring of suc
h domains. (C) 2001 Elsevier Science BN. All rights reserved.