Specific aptamer-protein interaction studied by atomic force microscopy.
Aptamers are a new class of synthetic DNA/RNA oligonucleotides 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.
Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.
Yaxin
Y
Jiang
Chuanfeng
C
Zhu
Liansheng
L
Ling
Lijun
L
Wan
Xiaohong
X
Fang
Chunli
C
Bai
D006801:Humans; D007073:Immunoglobulin E / Q000032:analysis; D018625:Microscopy, Atomic Force; D009841:Oligonucleotides / Q000737:chemistry*; D016012:Poisson Distribution; D011506:Proteins / Q000737:chemistry*
D009841:Oligonucleotides; D011506:Proteins; D007073:Immunoglobulin E