Fukushima D, Yokoyama S, Kroon D J, Kézdy F J, Kaiser E T
J Biol Chem. 1980 Nov 25;255(22):10651-7.
The segment corresponding to residues 121 to 164 of human plasma apolipoprotein A-I (apo-A-I) has been synthesized by the Merrifield solid phase method. The peptide binds to unilamellar phospholipid vesicles and to phospholipid-cholesterol mixed vesicles. The surface affinity of the peptide measured in this way indicated that the mechanism of binding is the same as that of apo A-I (144-165) and apo A-I itself. The peptide appears to be a globular monomer in a aqueous solution, with 17% alpha helix content. The peptide bound to vesicles activates lecithin:cholesterol acyltransferase: compared to apo A-I, the peptide is about 30% as efficient in the activation of cholesterol esterification and of phospholipid hydrolysis when the surface is saturated by the activator. For a variety of amphiphilic peptides and for apo A-I, the lecithin: cholesterol acyltransferase-activating ability correlates well with their alpha helix contents in 50% trifluoroethanol.
人血浆载脂蛋白A-I（apo-A-I）中对应于121至164位氨基酸残基的片段已通过梅里菲尔德固相法合成。该肽可与单层磷脂囊泡以及磷脂 - 胆固醇混合囊泡结合。通过这种方式测得的肽的表面亲和力表明，其结合机制与apo A-I（144 - 165）和apo A-I本身相同。该肽在水溶液中似乎是一种球状单体，α-螺旋含量为17%。与apo A-I相比，结合到囊泡上的该肽在激活卵磷脂：胆固醇酰基转移酶方面，当表面被激活剂饱和时，其在胆固醇酯化和磷脂水解激活方面的效率约为apo A-I的30%。对于多种两亲性肽和apo A-I而言，在50%三氟乙醇中，它们激活卵磷脂：胆固醇酰基转移酶的能力与其α-螺旋含量密切相关。
