Quantifying Biomolecular Interactions Using Slow Mixing Mode (SLOMO) Nanoflow ESI-MS
Duong T. Bui, Zhixiong Li, Pavel I. Kitov, Ling Han, Elena N. Kitova, Marlène Fortier, Camille Fuselier, Philippine Granger Joly de Boissel, David Chatenet, Nicolas Doucet, S. Mark Tompkins, Yves St‐Pierre, Lara K. Mahal, John S. Klassen
Abstract
to be calculated. The reliability of SLOMO and its ease of use is demonstrated through affinity measurements performed on peptide-antibiotic, protease-protein inhibitor, and protein oligomerization systems. Finally, affinities measured for the binding of human and bacterial lectins to a nanobody, a viral glycoprotein, and glycolipids displayed within a model membrane highlight the tremendous power and versatility of SLOMO for accurately quantifying a wide range of biomolecular interactions important to human health and disease.