Concentration‐dependent and surface‐assisted self‐assembly properties of a bioactive estrogen receptor α‐derived peptide. (22nd December 2014)

• Record Type: Journal Article
• Authors: Ruggeri, Francesco Simone; Byrne, Cillian; Khemtemourian, Lucie; Ducouret, Guylaine; Dietler, Giovanni; Jacquot, Yves
• Is Part Of: Journal of peptide science. Volume 21:Number 2(2015:Feb.)
• Page Start: 95
• Page End: 104
• Publication Date: 2014-12-22
• Subjects: Peptides -- Periodicals; Peptides -- Periodicals; 572.65
• DOI: 10.1002/psc.2730
• Languages: English
• ISSNs: 1075-2617

Abstract

<abstract abstract-type="main"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 &amp; Sons, Ltd.</p> </abstract>