Reversible Amyloid Fiber Formation in the N Terminus of Androgen Receptor

Most of the biological effects of androgen hormones are mediated through an intracellular transcription factor, the androgen receptor (AR). This protein presents a long disordered N‐terminal domain (NTD), known to aggregates into amyloid fibers.1 This aggregation property is usually associated with the presence of a poly‐glutamine tract (polyQ), known to be involved in several pathologies.2 The NTD has gain interest recently because potential anti‐prostate‐cancer molecules could target this domain.3 Here, we characterize a conserved region of the NTD (distal from polyQ); it promotes the formation of amyloid fibers under mild oxidative conditions. Unlike most fibrils, which are irreversibly aggregated, the free peptides can be restored from the fibril by the addition of a reducing agent.