α -lactalbumin (α-LA) is known as partly integral protein at acidic pH, and it has an amphipathic helix. Thus the interaction between α-LA and liposome produces various result.
When the liposome is composed of dimirystoyl phosphatidylcholine (DMPC), α-LA can micellize the the liposome of low lipid/protein molar ratios.
The micellization of DMPC SUV Induced by α-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.
protein 에 의한 liposome의 micellization을 연구하기위해 $\alpha$-lactalbumin dimirystoyl phosphatidylcholine small unilamellar vesicle을 이용하여 그들 상호작용을 관찰하였다. micellization process는 크게 3단계로 이루어지며 2가지 다른 s의 micellar complex가 존재한다. micellization process 에서는 항상 3kD si peptide가 phospholipid 와 hydrophobic interaction을 하고있다. 이 peptide $\alpha$-lactalbumin의 Phe-80 에서 Lys-108 부위인 것같다. 이 region은 amphipathic helix를 이룰 수 있다. lipid - protein interaction 의 결과에는 phospholipic head group도 중요한 역할을 한다.
