Probing fibronectin-antibody interactions using AFM force spectroscopy and lateral force microscopy

The first experiment showing the effects of specific interaction forces using lateral force microscopy (LFM) was demonstrated for lectin-carbohydrate interactions some years ago. Such measurements are possible under the assumption that specific forces strongly dominate over the non-specific ones. However, obtaining quantitative results requires the complex and tedious calibration of a torsional force. Here, a new and relatively simple method for the calibration of the torsional force is presented. The proposed calibration method is validated through the measurement of the interaction forces between human fibronectin and its monoclonal antibody. The results obtained using LFM and AFM-based classical force spectroscopies showed similar unbinding forces recorded at similar loading rates. Our studies verify that the proposed lateral force calibration method can be applied to study single molecule interactions.


Published in:
Beilstein Journal Of Nanotechnology, 6, 1164-1175
Year:
2015
Publisher:
Frankfurt Am Main, Beilstein-Institut
ISSN:
2190-4286
Keywords:
Laboratories:




 Record created 2015-09-28, last modified 2018-03-17


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