PMID- 15518395
OWN - NLM
STAT- MEDLINE
DCOM- 20050302
LR  - 20190715
IS  - 1533-4880 (Print)
IS  - 1533-4880 (Linking)
VI  - 4
IP  - 6
DP  - 2004 Jul
TI  - Study of the effect of metal ion on the specific interaction between protein and 
      aptamer by atomic force microscopy.
PG  - 611-5
AB  - We have studied the effect of metal ions on the specific interaction between a 
      protein, immunoglobulin E (IgE), and its 37-nt DNA aptamer with atomic force 
      microscopy (AFM). Protein aptamers are a new class of synthetic single-stranded 
      DNA/RNA oligonucleotide generated from in vitro selection to selectively bind 
      with target proteins. The IgE aptamers have been developed and are expected to be 
      promising reagents in IgE detection and new anti-allergic drug development. It is 
      known that the presence of metal ions in the buffer usually has a strong effect 
      on the affinity of single-stranded DNA for protein. In this work, the effect of 
      two representative monovalent ion and divalent ion on the binding of IgE and the 
      aptamer has been studied at the single-molecule level. The results from the AFM 
      force measurements show that the metal ions not only reduce the single-molecular 
      rupture force but also reduce the number of bonds formed between IgE and the 
      aptamer.
FAU - Jiang, Yaxin
AU  - Jiang Y
AD  - Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.
FAU - Wang, Jun
AU  - Wang J
FAU - Fang, Xiaohong
AU  - Fang X
FAU - Bai, Chunli
AU  - Bai C
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Nanosci Nanotechnol
JT  - Journal of nanoscience and nanotechnology
JID - 101088195
RN  - 0 (Ions)
RN  - 0 (Metals)
RN  - 0 (Peptides)
RN  - 0 (Proteins)
RN  - 37341-29-0 (Immunoglobulin E)
RN  - 9007-49-2 (DNA)
RN  - 9NEZ333N27 (Sodium)
RN  - I38ZP9992A (Magnesium)
SB  - IM
MH  - DNA/chemistry
MH  - Dose-Response Relationship, Drug
MH  - Fluorescence Polarization/*methods
MH  - Immunoglobulin E/chemistry
MH  - *Ions
MH  - Magnesium/chemistry
MH  - Metals/chemistry
MH  - Microscopy, Atomic Force/*methods
MH  - Nanotechnology/*methods
MH  - Peptides/*chemistry
MH  - Protein Binding
MH  - Proteins/*chemistry
MH  - Sodium/chemistry
EDAT- 2004/11/03 09:00
MHDA- 2005/03/03 09:00
CRDT- 2004/11/03 09:00
PHST- 2004/11/03 09:00 [pubmed]
PHST- 2005/03/03 09:00 [medline]
PHST- 2004/11/03 09:00 [entrez]
AID - 10.1166/jnn.2004.007 [doi]
PST - ppublish
SO  - J Nanosci Nanotechnol. 2004 Jul;4(6):611-5. doi: 10.1166/jnn.2004.007.