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BMC Bioinformatics

, 8:S20

First Online: 01 November 2007

Abstract

BackgroundThe UNO-RIC Nanopore Detector provides a new way to study the binding and conformational changes of individual antibodies. Many critical questions regarding antibody function are still unresolved, questions that can be approached in a new way with the nanopore detector.

ResultsWe present evidence that different forms of channel blockade can be associated with the same antibody, we associate these different blockades with different orientations of -capture- of an antibody in the detector-s nanometer-scale channel. We directly detect the presence of antibodies via reductions in channel current. Changes to blockade patterns upon addition of antigen suggest indirect detection of antibody-antigen binding. Similarly, DNA-hairpin anchored antibodies have been studied, where the DNA linkage is to the carboxy-terminus at the base of the antibody-s Fc region, with significantly fewer types of lengthy capture blockades than was observed for free un-bound IgG antibody. The introduction of chaotropic agents and its effects on protein-protein interactions have also been observed.

ConclusionNanopore-based approaches may eventually provide a direct analysis of the complex conformational -negotiations- that occur upon binding between proteins.

Electronic supplementary materialThe online version of this article doi:10.1186-1471-2105-8-S7-S20 contains supplementary material, which is available to authorized users.

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Autor: Stephen Winters-Hilt - Eric Morales - Iftekhar Amin - Alexander Stoyanov

Fuente: https://link.springer.com/







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