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Updated: Sep 17, 2025

Real Time Measurements of Membrane Protein:Receptor Interactions Using Surface Plasmon Resonance SPR
Published on: November 29, 2014
Broad-Spectrum Diffusion Coefficient Measurements via Surface Plasmon Resonance: From Thermodynamics to Protein
Giuseppe Stefano Basile1,2, Damiano Calcagno3, Nunzio Tuccitto1
1Department of Chemical Sciences, University of Catania, Viale Andrea Doria 6, 95125, Catania, Italy.
Abstract:
Information regarding the dimension and the shape of molecules in solution represents a holy grail for chemists. Recently, newly designed surface plasmon resonance (SPR) methods to precisely measure the diffusion coefficients (D) (D-SPR) have been developed and applied successfully to a variety of molecules, ranging from diverse long-chain alcohols to protein conformers and oligomers involved in conformational disorders, mostly represented by neurodegenerative processes of nervous tissues of the brain and retina. The dependence of D on the molecular size, shape, and oligomerization state of different molecules has been widely investigated, opening up new avenues and tools for chemical, biochemical, and clinical research. Herein, the historical basis and the development of the newly proposed D-SPR method are briefly described to obtain meaningful information about molecular features that are otherwise hard to characterize using more common and traditional bioanalytical approaches.
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