Force Spectroscopy of Polyclonal and Monoclonal Anti-Bovine Serum Albumin Antibodies - BSA Complexes

• Authors: L. Chtcheglova , G. Dietler
• Languages of publication: EN

Abstracts

EN

The specific interactions between bovine serum albumin and poly- or two monoclonal bovine serum albumin antibodies were studied using force spectroscopy mode of atomic force microscopy. The histograms of the unbinding forces for polyclonal bovine serum albumin antibodies are broad at high antibody concentrations (50 or 270 μg/ml) and narrow at low concentrations (10 or 27 μg/ml), while the histograms for monoclonal antibodies peak at well defined unbinding force. The peak unbinding force depends on the type of antibody and the antibody concentration. In this paper we described and characterized the passive adsorption and covalent immobilization of proteins for tip and sample preparation. Force spectroscopy could serve as a useful method for characterization of antigen-antibody interactions for measuring the specificity of an antibody or to assess the purity of a monoclonal antibody solution and to distinguish between different antibodies.

Keywords

EN

82.37.Gk; 82.37.Rs

Discipline

• 82.37.Gk: STM and AFM manipulations of a single molecule(for atom manipulation see 37.10.Gh, Pq in atomic and molecular physics; see also 81.16.Ta Atom manipulation in methods of nanofabrication and processing; 87.80.Nj Single-molecule techniques in biological physics)
• 82.37.Rs: Single molecule manipulation of proteins and other biological molecules

• Journal: Acta Physica Polonica A
• Year: 2003
• Volume: 104
• Issue: 3-4
• Pages: 321-326

Dates

published

2003-09/10

received

2003-07-16

Contributors

author

L. Chtcheglova

• Institut de Physique de la Matière Condensée, University of Lausanne, 1015 Lausanne, Switzerland

author

G. Dietler

• Institut de Physique de la Matière Condensée, University of Lausanne, 1015 Lausanne, Switzerland

References

• 1. P. Hinterdorfer, W. Baumgartner, H.J. Gruber, K. Schilcher, H. Schindler, Proc. Natl. Acad. Sci. USA, 93, 3477, 1996
• 2. J. Dammer, M. Hegner, D. Anselmetti, P. Wagner, D. Dreier, W. Huber, H.-J. Güntherodt, Biophys. J., 70, 2437, 1996
• 3. J.P. Cleveland, S. Manne, D. Bocek, P.K. Hansma, Rev. Sci. Instrum., 64, 403, 1993
• 4. J.L. Hutter, J. Bechhoefer, Rev. Sci. Instrum., 64, 1868, 1993
• 5. U. Jonsson, G. Olofsson, M. Malmqvist, I. Ronnberg, Thin Solid Films, 124, 117, 1985
• 6. E.T. Vandenberg, L. Bertilsson, B. Lieberg, K. Uvdal, R. Erlandsson, H. Elwing, I. Lundstrom, J. Colloid Interface Sci., 147, 322, 1991
• 7. Y.L. Lyubchenko, A.A. Gall, L.S. Shlyakhtenko, R.E. Harrington, B.L. Jacobs, P.I. Oden, S.M. Lindsay, J. Biomol. Struct. Dyn., 10, 589, 1992
• 8. Y.L. Lyubchenko, R.E. Blankenship, S.M. Lindsay, L.S. Shlyakhtenko, Scanning Microscopy, 10, 1997, 1996
• 9. L.S. Shlyakhtenko, A.A. Gall, J.J. Weimer, D.D. Hawn, Y.L. Lyubchenko, Biophys. J., 77, 568, 1999
• 10. E.T. Vandenberg, L. Bertilsson, B. Liedberg, K. Uvdal, R. Erlandsson, H. Elwing, I. Lundström, J. Colloid Interface Sci., 147, 103, 1991
• 11. T. Vallant, H. Brunner, U. Mayer, P. Hoffmann, T. Leitner, R. Resch, G. Friedbacher, J. Phys. Chem. B, 102, 7190, 1998
• 12. S. Kasas, B.M. Riederer, S. Catsicas, B. Cappella, G. Dietler, Rev. Sci. Instrum., 71, 2082, 2000

Identifiers

DOI

10.12693/APhysPolA.104.321