We use surface plasmon resonance (Biacore T100 and Biacore J) to analyze binding properties of ligands to receptor molecules. Here, the receptor molecules are immobilized on the surface with various immobilization protocols. Interactions between ligands and proteins can be measured by the surface plasmon resonance analysis to determine the binding affinity. Binding kinetics can often also be determined. Distinction between specific and non-specific binding is easily possible.
Phenylthiazolyl-Hydrazide and Its Derivatives Are Potent Inhibitors of τ Aggregation and Toxicity in Vitro and in Cells,
Marcus Pickhardt, Gregor Larbig, Inna Khlistunova, Atilla Coksezen, Bernd Meyer, Eva-Maria Mandelkow, Boris Schmidt, and Eckhard Mandelkow,
Biochemistry; 46, 10016 – 10023, (2007).
Discovery and Optimization of a Natural HIV-1 Entry Inhibitor Targeting the gp41 Fusion Peptide
Jan Münch, Ludger Ständker, Knut Adermann, Axel Schulz, Michael Schindler, Raghavan Chinnadurai, Stefan Pöhlmann, Chawaree Chaipan, Thorsten Biet, Thomas Peters,
Bernd Meyer, Dennis Wilhelm, Hong Lu, Weiguo Jing, Shibo Jiang, Wolf-Georg Forssmann, and Frank Kirchhoff,
Cell 129, 263–275, ( 2007).