Protein-Antibody Interactions Measured by AFM
Frediani C.*, a, S. Loia, M. Ruffaa, P. Baschieria, B. Cappellaa, G. Cercignanib, P. Pelosic, D. Petracchia, C.Ascolia
aIstituto di Biofisica, C.N.R.,
bDipartimento di Fisiologia e Biochimica, Università di Pisa, Italy
cDipartimento di Chimica e Biotecnologie Agrarie, Università di Pisa, Italy.
This is an abstract
for a presentation given at the
Foresight Conference on Molecular Nanotechnology.
There will be a link from here to the full article when it is
available on the web.
Specific interactions between Odorant Binding Protein (OBP) and its polyclonal antibodies have been evaluated from force-distance curves acquired with an atomic force microscope (AFM). Several control experiments have been included to verify the specificity of the interactions. From the acquired force-distance curves, an average rupture force of 50 pN has been calculated for individual antibody-antigen complexes. Moreover the number of curves with at least one specific detachment (nc) and the number of bonds measured in 800 force-distance curves (nb) have been studied as function of the contact time between tip and sample. A simple probabilistic model for the formation of OBP-antibody bonds allows to account for the trend of both nc and nb and to evaluate the number of antibody molecules on the tip.
Istituto di Biofisica, C.N.R.
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