Influence of lipid composition on the interaction of apolipoprotein model peptides with liposomes

被引：0
|
作者：
Wang, QD [1 ]
Cui, DF [1 ]
Lin, QS [1 ]
机构：
[1] ACAD SINICA,SHANGHAI INST BIOCHEM,STATE KEY LAB MOL BIOL,SHANGHAI 200031,PEOPLES R CHINA
来源：
ACTA BIOCHIMICA ET BIOPHYSICA SINICA | 1996年 / 28卷 / 06期
关键词：
amphiphilic peptide; liposome; peptide-lipid interaction; lipid composition;
D O I：
暂无
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Two amphiphilic peptides, Amp1 and Amp2, were synthesized according to the sequence of the lipid binding domain in apolipoprotein. Amp2 has a Val residue substituted for the Lys at the 4th position of Amp1. Interactions between Amp1 or Amp2 and liposomes with different lipid compositions were compared by studying the blue shifts of the intrinsic fluorescence emission maxima, the peptide-induced liposome leakage and the quenching of tryptophan fluorescence by acrylamide. The influence of temperature on interactions was studied as mall. Amp1 interacted stronger with acidic lipids while Amp2 interacted stronger with zwitterionic lipids. The interaction was reinforced mi Lih the increasing extent of lipid unsaturation as well as with the increase of temperature. The lipid unsaturation had a more prominent effect.
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页码：624 / 632
页数：9
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