Concentration‐dependent and surface‐assisted self‐assembly properties of a bioactive estrogen receptor α‐derived peptide | Zendy

Ruggeri Francesco Simone | Zendy; Byrne Cillian | Zendy; Khemtemourian Lucie | Zendy; Ducouret Guylaine | Zendy; Dietler Giovanni | Zendy; Jacquot Yves | Zendy

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research