2-DIMENSIONAL ASSEMBLY FORMATION OF HYDROPHOBIC HELICAL PEPTIDES AT THE AIR-WATER-INTERFACE - FLUORESCENCE MICROSCOPIC STUDY
2-DIMENSIONAL ASSEMBLY FORMATION OF HYDROPHOBIC HELICAL PEPTIDES AT THE AIR-WATER-INTERFACE - FLUORESCENCE MICROSCOPIC STUDY
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DOI：
10.1021/la00001a043
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发表时间：
1995-01-01
期刊：
影响因子：
3.9
通讯作者：
RINGSDORF, H
中科院分区：
文献类型：
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作者：
FUJITA, K;KIMURA, S;RINGSDORF, H
用荧光显微镜研究了疏水性α-螺旋肽X-(Ala-Alb)(8)-Y(X=Boc-，HOOCCH_2CH_2CO-，biotinyl，biotinyl-(Sar)(3)-；Y=OMe，OBzl，OH)在空气/水界面上的单层形成。有些多肽在pi-A等温线上出现丘状。当将含有少量FITC标记多肽的单层保持在与丘顶对应的表面压力下时，荧光显微镜下观察到明亮和黑暗的结构域。通过将阳离子染料(DIIC(1))添加到多肽单分子层下面的亚相中，也观察到了结构域的形成。因此，pi-A等温线中的丘状结构归因于从膨胀态到凝聚态的相变。根据多肽在单层中的不同取向，观察和讨论了两种不同形状的固体结构域(叶状和针状)。
Monolayer formation of hydrophobic a-helical peptides, X-(Ala-Aib)(8)-Y (X = Boc-, HOOCCH2CH2CO-, biotinyl, biotinyl-(Sar)(3)-; Y = OMe, OBzl, OH), at the air/water interface was studied by the fluorescence microscopic method. Some peptides showed a mound in the pi-A isotherm. When the monolayer containing a small amount of FITC-labeled peptide was held at the surface pressure corresponding to the top of the mound, bright and dark domains were observed by fluorescence microscopy. Domain formation was also observed by the addition of a cationic dye (DiIC(1)) into the subphase underneath the peptide monolayer. The mound in the pi-A isotherm is, therefore, ascribed to the phase transition from an expanded state to a condensed state. Two different shapes (leaflet and needle) of solid domains were observed and discussed in terms of different orientations of the peptides in the monolayer.