The elucidation of the structure and dynamics of amyloid assemblies associated with disease has been elusive. Here we show that by using ligand-detected NMR, one can obtain structural and dynamical information on assemblies formed by amylin associated with type 2 diabetes. The binding mode of the ligand as indicated by chemical shift perturbation data strongly depend on the state of amylin assembly. Dynamics in the form of relaxation rates and diffusion coefficients of bound ligands yield insight into assembly size. Figure 1. <img src='https://acs-archive-assets2.s3.amazonaws.com/239nm/uploads/5170_irciniastatin_a.jpg' alt='' />

Using ligand-detected NMR to probe the aggregation of amylin

240th National Meeting (2010)

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