Intrinsically Disorded Proteins
Intrinsically disordered proteins or proteins with intrinsically disordered domains are highly abundant. Often such proteins tend to aggregate in higher concentration and especially when they are not bound by any ligand. Using liposome tethered IDPs together with our dISA technology allows to determine the binding kinetics of various ligands straightforward. Another advantage comes to play when one is looking at IDPs and protein protein interactions (PPI). Our dISA technology allows to resemble the targeted PPI (see PPI page) and thereby we can determine the impact of any ligand on the PPI. The outstanding sensitivity of our single molecule microscopy based dISA technology is able to detect even subtle changes of the targeted PPI. This differentiates dISA clearly from other label free technologies that in a direct binding assay can only detect binding to one of the proteins without any functional readout. Inhibition in solution assays can give a functional response but the binding kinetics of the ligand cannot be detected and high amounts of protein are needed. The dISA technology requires only minute amounts of protein since the typicalprotein concentration is femto- to picomolar and the used volumes are small, usually 10-20μL.