title: Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptide.
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.
authors.affiliation: Laboratoire de Physique de la Matière Vivante, Institut de Physique des Systèmes Biologiques, Ecole Polytechnique Fédérale de Lausanne, CH-1015, Lausanne, Switzerland.
authors.forename: Francesco Simone
authors.initials: FS
authors.lastname: Ruggeri
authors.forename: Cillian
authors.initials: C
authors.lastname: Byrne
authors.forename: Lucie
authors.initials: L
authors.lastname: Khemtemourian
authors.forename: Guylaine
authors.initials: G
authors.lastname: Ducouret
authors.forename: Giovanni
authors.initials: G
authors.lastname: Dietler
authors.forename: Yves
authors.initials: Y
authors.lastname: Jacquot
mesh_terms: D000682:Amyloid / Q000737:chemistry / Q000378:metabolism; D049109:Cell Proliferation / Q000187:drug effects; D004305:Dose-Response Relationship, Drug; D047628:Estrogen Receptor alpha / Q000737:chemistry*; D006801:Humans; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate / Q000737:chemistry / Q000378:metabolism; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism* / Q000494:pharmacology; D017433:Protein Structure, Secondary; D013499:Surface Properties
chemical_list: D000682:Amyloid; D047628:Estrogen Receptor alpha; D010446:Peptide Fragments; D020136:Hydrogel, Polyethylene Glycol Dimethacrylate
keywords: amyloid-like fibrils; estrogen receptor; hydrogel; microscopy; peptide; rheology; spectroscopy