Journal of Peptide Science · 2014 · 24 citations · 43 references
Life SciencesBiochemistryBiophysicsBiophysical ChemistryMolecular BiophysicsStructural BiologyAmyloid FormationGelsHydrogelsMacromolecular AssemblyPeptide ChemistryProtein StructureAmyloid Fibril FormationAmyloid Fibril StructureAmyloid FibrilsAmyloid StructureElectrostatic InteractionsHinge Region StructureRheological BehaviorSelf-assembling Peptide Hydrogels
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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