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The added-values of IDAP

How does IDAP work? As illustrated below, IDAP involves plasmids, derived from a proprietary vector backbone. A Target plasmid that contains a DNA element-of-interest to which one wishes to discover the specific binding proteins and the Control plasmid, devoid of that element, are separately immobilized on streptavidin coated magnetic beads via a triple helix-forming probe. The plasmid-bound beads are incubated in an extract of choice, under defined conditions of time and temperature.

Following incubation, both Target and Control plasmids are recovered on a magnet, submitted to a proprietary washing procedure to remove non-specific proteins. Subsequently, protein assembled on DNA are analyzed by Mass Spectrometry or Western Blotting. Identification of proteins specifically assembled on the DNA element-of-interest is implemented by comparing proteins bound to Target and Control plasmid. The IDAP approach is versatile and robust, however it is a screen that needs further validation of the discovered hits by biochemical and/or genetic experiments.


Robustness of IDAP is best characterized by a low background of unspecific proteins. Remarkable features of IDAP entail: i) its extended linker allowing the attachment of the plasmid via triple-helix formation thus avoiding that heat-denaturation steps commonly used in Watson-Crick hybridization, ii) Circular plasmids are immobilized thus preventing exonucleolytic degradation in extracts, iii) Proprietary washing procedure (protected by Know-How) strongly reducing the background.

Most diseases result from a defect in gene expression. IDAP methodology allows the proteins involved to be detected, thus providing novel pharmacological targets.

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