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Concentration‐dependent and surface‐assisted self‐assembly properties of a bioactive estrogen receptor α‐derived peptide
Author(s) -
Ruggeri Francesco Simone,
Byrne Cillian,
Khemtemourian Lucie,
Ducouret Guylaine,
Dietler Giovanni,
Jacquot Yves
Publication year - 2015
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2730
Subject(s) - peptide , fibril , estrogen receptor , estrogen , biophysics , chemistry , rheology , receptor , atomic force microscopy , biochemistry , nanotechnology , materials science , medicine , biology , endocrinology , cancer , breast cancer , composite material
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.