ArticleBiophysical journal2008
Deciphering the energy landscape of the interaction uranyl-DCP with antibodies using dynamic force spectroscopy.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Exploring the energy profile of human IgG/rat anti-human IgG interactions by dynamic force spectroscopy.The protein journal · 2012Article
- DeStripe: frequency-based algorithm for removing stripe noises from AFM images.BMC structural biology · 2011Article
- Predicting the disruption by UO2(2+) of a protein-ligand interaction.Protein science : a publication of the Protein Society · 2010Article
- Methods and estimations of uncertainties in single-molecule dynamic force spectroscopy.European biophysics journal : EBJ · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies on molecular recognition of uranyl-DCP (dicarboxy-phenanthroline chelator) compound by two distinct monoclonal antibodies (Mabs U04S and U08S) clearly showed the presence of a biphasic shape in Bell-Evans' plots and an accentuated difference in slopes at the high loading rates. To further explore the basis in the slope difference, we have performed complementary experiments using antibody PHE03S, raised against uranyl-DCP but, presenting a strong cross-reactivity toward the DCP chelator. This work allowed us to obtain a reallocation of the respective contributions of the metal ion itself and that of the chelator. Results led us to propose a 2D schematic model representing two energy barriers observed in the systems Mabs U04S- and U08S-[UO(2)-DCP] where the outer barrier characterizes the interaction between UO(2) and Mab whereas the inner barrier characterizes the interaction between DCP and Mab. Using dynamic force spectroscopy, it is thus possible to dissect molecular interactions during the unbinding between proteins and ligands.
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