Keeping it all together

Several neurodegenerative diseases, such as Alzheimer disease, are associated with the deposition of misfolded or misassembled proteins into fibrous -sheet aggregates known as amyloid. The oligomeric dissociation of transthyretin (TTR), a tetrameric thyroxane (T4) transporter protein found in serum and cerebrospinal fluid, is the rate-limiting step for fibril formation associated with several amyloid diseases. Wiseman et al. have recently shown in the Journal of the American Chemical Society that an inhibitor of fibril formation tethered to TTR by a disulfide bond can block the dissociation of TTR's native structure.