Abstract
Monolayers of a protein β-lactoglobulin (βL) and two lipids distearoylphosphatidylcholine (DSPC) and dimirystoylphosphatidylcholine (DMPC) on aqueous subphase containing Na+ or Ca2+ ions are studied. The spreading isotherms and the ATR-FTIR spectra of LB plurilayers transferred, allow to deduce that α-helix conformation of β-lactoglobulin is the prevailing form. The study of bidimensional mixtures between βL with DSPC and with DMPC shows that the components are incompatible at the W/A interface.
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