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Updated: Apr 19, 2026

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
Published on: December 19, 2018
Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived
Francesco Simone Ruggeri1, Cillian Byrne, Lucie Khemtemourian
1Laboratoire de Physique de la Matière Vivante, Institut de Physique des Systèmes Biologiques, Ecole Polytechnique Fédérale de Lausanne, CH-1015, Lausanne, Switzerland.
Abstract:
We have synthesized a 17-mer peptide (ERα17p) that is issued from the hinge region of the estrogen receptor α and which activates the proliferation of breast carcinoma cells in steroid-deprived conditions. In the present paper, we show that at a concentration of ~50 μM, it rapidly forms amyloid-like fibrils with the assistance of electrostatic interactions and that at higher concentrations, it spontaneously forms a hydrogel. By using biophysical, spectral and rheological techniques, we have explored the structural, biophysical and mechanical characteristics of ERα17p with respect to fibril formation and gelation.
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