Investigation of the Assembly Behavior of an Amphiphilic Lipopeptide at the Liquid Crystal-Aqueous Interface

被引：21

作者：

Yang, Xiuxiu ^{[1
]}

Tan, Yi ^{[1
]}

Li, Fangyi ^{[2
]}

Yu, Qing ^{[2
]}

Tan, Suk Fun ^{[1
]}

Chen, Yongxiang ^{[2
]}

Yang, Zhongqiang ^{[1
]}

机构：

[1] Tsinghua Univ, Dept Chem, Minist Educ, Key Lab Organ Optoelect & Mol Engn, Beijing 100084, Peoples R China

[2] Tsinghua Univ, Dept Chem, Minist Educ, Key Lab Bioorgan Phosphorus Chem & Chem Biol, Beijing 100084, Peoples R China

来源：

LANGMUIR | 2019年 / 35卷 / 07期

基金：

中国国家自然科学基金;

关键词：

ORDERING TRANSITIONS; DNA; BINDING; REORIENTATION; PRINCIPLES; MOLECULES; DROPLETS;

D O I：

10.1021/acs.langmuir.8b03294

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

In this article, we designed an amphiphilic lipopeptide molecule, 5(6)-carboxyfluorescein-KKKKKKSKTK-Cys(C12H25)-OMe (FAM-lipopeptide-C12), and studied its assembly behavior at the 4-cyano-4'-pentylbiphenyl (5CB)-aqueous interface. The ordering transitions of liquid crystals (LCs) revealed that FAM-lipopeptide-C12 can assemble at the LC-aqueous interface (both planar and curved interfaces). The assembly can be destroyed by adding trypsin, which catalyzes the hydrolysis of lipopeptides. Fluorescence measurements further confirmed the assembly and deassembly behavior of FAM-lipopeptide-C12 at the LC-aqueous interface. Overall, our work provides a general method for the construction of a biointerface by directly assembling amphiphilic lipopeptides at the LC-aqueous interface, which can potentially be used in selectively detecting the activity of specific enzymes and other biomolecular interactions.

引用

页码：2490 / 2497

页数：8

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