Specific aptamer-protein interaction studied by atomic force microscopy

被引：118

作者：

Jiang, YX

Zhu, CF

Ling, LS

Wan, LJ

Fang, XH ^{[1
]}

Bai, C

机构：

[1] Chinese Acad Sci, Inst Chem, Beijing 100080, Peoples R China

[2] Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China

来源：

ANALYTICAL CHEMISTRY | 2003年 / 75卷 / 09期

关键词：

D O I：

10.1021/ac026182s

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Aptamers are a new class of synthetic DNA/RNA oligo-nucleotides generated from in vitro selection to selectively bind with various molecules. Due to their molecular recognition capability for proteins, aptamers are becoming promising reagents in protein detection and new drug development. In this study, the specific interaction between the protein immunoglobulin E (IgE) and its 37-nt aptamer has been measured directly by atomic force microscopy. The single-molecule unbinding force between IgE and the aptamer is determined using the Poisson statistical method. The individual unbinding force between IgE and its monoclonal antibody has also been obtained and compared to that between IgE and the aptamer. The results reveal the high affinity of the aptamer to protein, which could match or even surpass that of the antibody to its antigen.

引用

页码：2112 / 2116

页数：5

共 44 条

[1] Detection of antigen-antibody binding events with the atomic force microscope [J].