Concentration‐dependent and surface‐assisted self‐assembly properties of a bioactive estrogen receptor α‐derived peptide |
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| Authors: | Lucie Khemtemourian Guylaine Ducouret Giovanni Dietler Yves Jacquot |
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| Affiliation: | 1. Ecole Normale Supérieure, Département de Chimie, Sorbonne Universités – UPMC Univ Paris 06, CNRS UMR 7203, Paris, France;2. Laboratoire de Physico‐chimie des Polymères et Milieux Dispersés, CNRS UMR 7615, Ecole Supérieure de Physique et de Chimie de la ville de Paris (ESPCI), Paris Cedex 05, France;3. Laboratoire de Physique de la Matière Vivante, Institut de Physique des Systèmes Biologiques, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland |
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| 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. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | estrogen receptor peptide spectroscopy microscopy rheology amyloid‐like fibrils hydrogel |
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