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

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

doi:10.1002/psc.2730

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

Francesco Simone Ruggeri, Cillian Byrne, Lucie Khemtemourian, Guylaine Ducouret, Giovanni Dietler, Yves Jacquot^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

20 Citations (Scopus)

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.

Original language	English
Pages (from-to)	95-104
Number of pages	10
Journal	Journal of Peptide Science
Volume	21
Issue number	2
DOIs	https://doi.org/10.1002/psc.2730
Publication status	Published - Feb 2015
Externally published	Yes

Keywords

Amyloid-like fibrils
Estrogen receptor
Hydrogel
Microscopy
Peptide
Rheology
Spectroscopy

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10.1002/psc.2730

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title = "Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptide",

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.",

keywords = "Amyloid-like fibrils, Estrogen receptor, Hydrogel, Microscopy, Peptide, Rheology, Spectroscopy",

author = "Ruggeri, {Francesco Simone} and Cillian Byrne and Lucie Khemtemourian and Guylaine Ducouret and Giovanni Dietler and Yves Jacquot",

year = "2015",

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T1 - Concentration-dependent and surface-assisted self-assembly properties of a bioactive estrogen receptor α-derived peptide

AU - Ruggeri, Francesco Simone

AU - Byrne, Cillian

AU - Khemtemourian, Lucie

AU - Ducouret, Guylaine

AU - Dietler, Giovanni

AU - Jacquot, Yves

PY - 2015/2

Y1 - 2015/2

N2 - 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.

AB - 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.

KW - Amyloid-like fibrils

KW - Estrogen receptor

KW - Hydrogel

KW - Microscopy

KW - Peptide

KW - Rheology

KW - Spectroscopy

U2 - 10.1002/psc.2730

DO - 10.1002/psc.2730

M3 - Article

C2 - 25530026

AN - SCOPUS:84921823563

SN - 1075-2617

VL - 21

SP - 95

EP - 104

JO - Journal of Peptide Science

JF - Journal of Peptide Science

IS - 2

ER -

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

Abstract

Keywords

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