Comparative interaction of ?-helical and ?-sheet amphiphilic isopeptides with phospholipid monolayers
Comparative interaction of ?-helical and ?-sheet amphiphilic isopeptides with phospholipid monolayers
复制标题
β-螺旋和β-片层两亲异肽与磷脂单层的相互作用比较
DOI:
10.1002/1097-0282(200107)59:1
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发表时间:
2001
期刊:
影响因子:
2.9
通讯作者:
D. Lelièvre
中科院分区:
文献类型:
--
作者:
R. Maget;D. Lelièvre
The two sequential amphiphilic peptide isomers, (Leu-Lys-Lys-Leu)4 and (Leu-Lys)8, were chosen as models for alpha-helical and beta-sheet peptides, respectively. In order to evaluate the contribution of the secondary structure of a peptide to its penetration into cellular membranes, interactions of these isopeptides with L-alpha-dimyristoyl phosphatidylcholine (DMPC) monolayers were studied. Both isopeptides penetrate into DMPC monolayers up to an exclusion pressure of approximately 27 mN/m, but a discontinuity is observed in the penetration profile of the alpha-helical (LKKL)4. The main parameters extracted from the compression isotherms of the mixed peptide/DMPC monolayers-namely, transition pressure, mean area, elasticity modulus, and energy of mixing-were analyzed. These analyses indicate that the alpha-helical isomer interacts strongly with DMPC by forming a 1:32 (LKKL)4-DMPC complex. When engaged in this complex, (LKKL)(4) behaves as an hydrophobic helix and has a tendency to become vertically oriented in the course of the compression process. The beta-sheet (LK)8 interacts more weakly with DMPC and no complex can be detected.
影响因子:
3.4
作者:
DEGRADO, WF;MUSSO, GF;KEZDY, FJ
通讯作者:
KEZDY, FJ
DOI:
10.1111/j.1432-1033.1996.0243r.x
发表时间:
1996
期刊:
European journal of biochemistry
影响因子:
--
作者:
Rodríguez-Crespo,I;Gómez-Gutiérrez,J;Encinar,JA;González-Ros,JM;Albar,JP;Peterson,DL;Gavilanes,F
通讯作者:
Gavilanes,F