Abstract
Monolayers of phosphatidylcholine, tyrosine, and phenylalanine and binary mixtures phosphatidylcholine-tyrosine or phosphatidylcholine-phenylalanine were investigated at the air/water interface. Phosphatidylcholine (lecithin, PC), tyrosine (Tyr), and phenylalanine (Phe) were used in the experiment. The surface tension values of pure and mixed monolayers were used to calculate π-A isotherms. The surface tension measurements were carried out at 22°C using an improved Teflon trough and a Nima 9000 tensiometer. The Teflon trough was filled with a subphase of triple-distilled water. Known amounts of lipid dissolved in 1-chloropropane were placed at the surface using a syringe. The interactions between lecithin and amino acid result in significant deviations from the additivity rule. An equilibrium theory to describe the behavior of monolayer components at the air/water interface was developed in order to obtain the stability constants of PC-Tyr as well as PC-Phe complexes. We considered the equilibrium between the individual components and the complex and established that lecithin and amino acid formed highly stable 1:1 complex.
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