Scanning Tunneling Microscope Observation of the Phosphatidylserine Domains in the Phosphatidylcholine Monolayer

被引：9

作者：

Matsunaga, Soichiro ^{[1
]}

Yamada, Taro ^{[2
]}

Kobayashi, Toshihide ^{[2
]}

Kawai, Maki ^{[1
]}

机构：

[1] Univ Tokyo, Dept Adv Mat Sci, Kashiwa, Chiba 2778561, Japan

[2] RIKEN, Lipid Biol Lab, Wako, Saitama 3510198, Japan

来源：

LANGMUIR | 2015年 / 31卷 / 19期

基金：

日本学术振兴会;

关键词：

MOLECULAR-DYNAMICS SIMULATION; LATERAL PHASE SEPARATIONS; MODEL MEMBRANES; ELECTRON-TRANSFER; LIPID RAFTS; ANNEXIN-V; BILAYER; FUSION; BINDING; VISUALIZATION;

D O I：

10.1021/acs.langmuir.5b00859

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A mixed monolayer of 1,2-dihexanoyl-sn-glycero-3-phospho-L-serine (DHPS) and 1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) on an 1-octanethiol-modified gold substrate was visualized on the nanometer scale using in situ scanning tunneling microscopy (STM) in aqueous solution. DHPS clusters were evident as spotty domains. STM enabled us to distinguish DHPS molecules from DHPC molecules depending on their electronic structures. The signal of the DHPS domains was abolished by neutralization with Ca2+. The addition of the PS + Ca2+-binding protein of annexin V to the Ca2+-treated monolayer gave a number of spots corresponding to a single annexin V molecule.

引用

页码：5449 / 5455

页数：7

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