Literature DB >> 9200694

Detection of antigen-antibody binding events with the atomic force microscope.

S Allen1, X Chen, J Davies, M C Davies, A C Dawkes, J C Edwards, C J Roberts, J Sefton, S J Tendler, P M Williams.   

Abstract

An atomic force microscope (AFM) has been used to directly monitor specific interactions between antibodies and antigens employed in an immunoassay system. Results were achieved using AFM probes functionalized with ferritin, and monitoring the adhesive forces between the probe and anti-ferritin antibody-coated substrates. Analysis of the force distribution data suggests a quantization of the forces, with a period of 49 +/- 10 pN. This periodic force may be attributed to single unbinding events between individual antigen and antibody molecules. These results demonstrate that the AFM could be employed as an analytical tool to study the interactions between the molecules involved in biosensor systems. The potential of the technique to provide information relating to the manner in which the antibody molecule binds to its specific antigen is also discussed.

Mesh:

Substances:

Year:  1997        PMID: 9200694     DOI: 10.1021/bi962531z

Source DB:  PubMed          Journal:  Biochemistry        ISSN: 0006-2960            Impact factor:   3.162


  51 in total

1.  Protein design is a key factor for subunit-subunit association.

Authors:  C Clementi; P Carloni; A Maritan
Journal:  Proc Natl Acad Sci U S A       Date:  1999-08-17       Impact factor: 11.205

2.  Protein adhesion force dynamics and single adhesion events.

Authors:  G Sagvolden
Journal:  Biophys J       Date:  1999-07       Impact factor: 4.033

3.  The influence of epitope availability on atomic-force microscope studies of antigen-antibody interactions.

Authors:  S Allen; J Davies; M C Davies; A C Dawkes; C J Roberts; S J Tendler; P M Williams
Journal:  Biochem J       Date:  1999-07-01       Impact factor: 3.857

4.  High-resolution imaging of antibodies by tapping-mode atomic force microscopy: attractive and repulsive tip-sample interaction regimes.

Authors:  A San Paulo; R García
Journal:  Biophys J       Date:  2000-03       Impact factor: 4.033

5.  Biomolecular interactions measured by atomic force microscopy.

Authors:  O H Willemsen; M M Snel; A Cambi; J Greve; B G De Grooth; C G Figdor
Journal:  Biophys J       Date:  2000-12       Impact factor: 4.033

6.  Temperature dependence of unbinding forces between complementary DNA strands.

Authors:  Irina Schumakovitch; Wilfried Grange; Torsten Strunz; Patricia Bertoncini; Hans-Joachim Güntherodt; Martin Hegner
Journal:  Biophys J       Date:  2002-01       Impact factor: 4.033

7.  Model energy landscapes and the force-induced dissociation of ligand-receptor bonds.

Authors:  T Strunz; K Oroszlan; I Schumakovitch; H Güntherodt; M Hegner
Journal:  Biophys J       Date:  2000-09       Impact factor: 4.033

8.  Unbinding forces of single antibody-antigen complexes correlate with their thermal dissociation rates.

Authors:  F Schwesinger; R Ros; T Strunz; D Anselmetti; H J Güntherodt; A Honegger; L Jermutus; L Tiefenauer; A Pluckthun
Journal:  Proc Natl Acad Sci U S A       Date:  2000-08-29       Impact factor: 11.205

9.  The effect of sedimentation and diffusion on cellular uptake of gold nanoparticles.

Authors:  Eun Chul Cho; Qiang Zhang; Younan Xia
Journal:  Nat Nanotechnol       Date:  2011-04-24       Impact factor: 39.213

10.  Force spectroscopy with a small dithering of AFM tip: a method of direct and continuous measurement of the spring constant of single molecules and molecular complexes.

Authors:  Lilia A Chtcheglova; George T Shubeita; Sergey K Sekatskii; Giovanni Dietler
Journal:  Biophys J       Date:  2004-02       Impact factor: 4.033

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.