(The) micellization of dimirystoyl phosphatidylcholine vesicle induced by α-lactalbumin at acidic pH

Abstract

$\alpha$ -lactalbumin ($\alpha$-LA) is known as partly integral protein at acidic pH, and it has an amphipathic helix. Thus the interaction between $\alpha$-LA and lipsome produces various result. When the liposome is composed of dimirystoyl phosphatidylcholine (DMPC), $\alpha$-LA can micellize the the liposome of low lipid/protein molar ratios. The micellization of DMPC SUV Induced by $\alpha$-LA result out two different sizes of micellar complex. The portions which are protected from tryptic digestion over all L/P ratios are Phe-80 to Lys-108. They are labelled with "$^{125}I$] TID. Thus they are hydrophobically interact with lipid core portion. They can form the amphiphatic helix.