Interaction of bundled ser-rich amphiphilic peptides with phospholipid membranes

被引:0
作者
Yoshida, K [1 ]
Ohmori, N [1 ]
Mukai, Y [1 ]
Niidome, T [1 ]
Hatakeyama, T [1 ]
Aoyagi, H [1 ]
机构
[1] Nagasaki Univ, Fac Engn, Dept Appl Chem, Nagasaki 8528521, Japan
关键词
bundled peptide; amphiphilic structure; membrane perturbation; membrane fusion; Trp titration;
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
To investigate properties of hydrophilic bundled peptides and their interactions with phospholipid membranes, bundled peptides named [Trp(2)]- and [Trp(12)]-4 alpha-4(6)S9, which are composed of four fragments of amphiphilic 24-mer peptide, were designed and synthesized, Tryptophan mp) was introduced at the 2nd position from the N-terminal or at the centre (12th) of the helix to monitor the peptide-lipid interaction. Circular dichroism measurements indicated that the peptides had low alpha-helicities in a buffer solution (pH 7.4) and also in the presence of dipalmitoyl-DL-3-phosphatidylcholine (DPPC) vesicles. In the presence of DPPC/dipalmitoyl-DL-3-phosphatidylglycerol (DPPG) (3:1) vesicles, the measurement could not be taken because of turbidity induced by vesicle aggregation. Both peptides had moderate perturbation activity for both the neutral and acidic vesicles at 25 degrees C. The perturbation patterns at 50 degrees C were much different from those at 25 degrees C and the maximum activity reached 100% at a low peptide concentration. The results of the measurement of membrane fusion activity of peptides showed a similar tendency to that found in the perturbation experiment, A quenching experiment indicated that the Trp(2) and Trp(12) residues in [Trp(2)]- and [Trp(12)]-4 alpha-4(6)S9 were scarcely embedded in neutral lipid membranes. Copyright (C) 1999 European Peptide Society and John Wiley & Sons, Ltd.
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页码:360 / 367
页数:8
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