Reversible amyloid fiber formation in the N terminus of androgen receptor

Chembiochem. 2014 Nov 3;15(16):2370-3. doi: 10.1002/cbic.201402420. Epub 2014 Sep 11.


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.

Keywords: amyloid beta-peptides; androgen receptor; dimerization; disulfide bridge; self-assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amyloid / chemistry*
  • Circular Dichroism
  • Dimerization
  • Humans
  • Male
  • Microscopy, Electron
  • Molecular Sequence Data
  • Peptides / chemistry
  • Protein Structure, Secondary
  • Receptors, Androgen / chemistry*
  • Receptors, Androgen / metabolism


  • Amyloid
  • Peptides
  • Receptors, Androgen
  • polyglutamine