Related ArticlesNMR WaterLOGSY Reveals Weak Binding of Bisphenol A with Amyloid Fibers of a Conserved 11 Residue Peptide from Androgen Receptor.
PLoS One. 2016;11(9):e0161948
Authors: Asencio-Hernández J, Kieffer B, Delsuc MA
Abstract
There is growing evidence that bisphenol A (BPA), a molecule largely released in the environment, has detrimental effects on ecosystems and on human health. It acts as an endocrine disruptor targeting steroid hormone receptors, such as the estrogen receptor (ER), estrogen-related receptor (ERR) and androgen receptor (AR). BPA-derived molecules have recently been shown to interact with the AR N-terminal domain (AR-NTD), which is known to be largely intrinsically disordered. This N-terminal domain contains an 11 residue conserved domain that forms amyloid fibers upon oxidative dimerisation through its strictly conserved Cys240 residue. We investigate here the interaction of BPA, and other potential endocrine disruptors, with AR-NTD amyloid fibers using the WaterLOGSY NMR experiment. We observed a selective binding of these compounds to the amyloid fibers formed by the AR-NTD conserved region and glutamine homopolymers. This observation suggests that the high potency of endocrine disruptors may result, in part, from their ability to bind amyloid forms of nuclear receptors in addition to their cognate binding sites. This property may be exploited to design future therapeutic strategies targeting AR related diseases such as the spinal bulbar muscular atrophy or prostate cancer. The ability of NMR WaterLOGSY experiments to detect weak interactions between small ligands and amyloid fibers may prove to be of particular interest for identifying promising hit molecules.
Conserved SecA Signal Peptide-Binding Site Revealedby Engineered Protein Chimeras and Fo?rster Resonance EnergyTransfer
Conserved SecA Signal Peptide-Binding Site Revealedby Engineered Protein Chimeras and Fo?rster Resonance EnergyTransfer
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01115/20160219/images/medium/bi-2015-011152_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01115
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/v7K1b408Q1s
More...
nmrlearner
Journal club
0
02-20-2016 11:00 AM
[NMR paper] Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Related Articles Backbone (1)H, (15)N, (13)C NMR assignment of the 518-627 fragment of the androgen receptor encompassing N-terminal and DNA binding domains.
Biomol NMR Assign. 2016 Jan 5;
Authors: Meyer S, Wang YH, Pérez-Escrivà P, Kieffer B
Abstract
Androgen receptor (AR) belongs to the nuclear receptor superfamily that are ligand dependent transcription factors. This protein binds to...
nmrlearner
Journal club
0
01-07-2016 11:10 PM
[NMR paper] Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Functional Binding Surface of a ?-Hairpin VEGF Receptor Targeting Peptide Determined by NMR Spectroscopy in Living Cells.
Chemistry. 2014 Nov 6;
Authors: Diana D, Russomanno A, Rosa LD, Di Stasi R, Capasso D, Di Gaetano S, Romanelli A, Russo L, D'Andrea LD, Fattorusso R
Abstract
In this study, the functional interaction of HPLW peptide with VEGFR2 (Vascular Endothelial Growth Factor Receptor 2) was determined...
nmrlearner
Journal club
0
11-08-2014 12:43 PM
[NMR paper] NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles NMR analysis of cross strand aromatic interactions in an 8 residue hairpin and a 14 residue three stranded ?-sheet peptide.
J Phys Chem B. 2012 Dec 13;116(49):14207-15
Authors: Sonti R, Rai R, Ragothama S, Balaram P
Abstract
Cross strand aromatic interactions between a facing pair of...
nmrlearner
Journal club
0
06-13-2013 06:14 PM
[NMR paper] The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
Related Articles The cellular prion protein traps Alzheimer's A? in an oligomeric form and disassembles amyloid fibers.
FASEB J. 2013 Jan 30;
Authors: Younan ND, Sarell CJ, Davies P, Brown DR, Viles JH
Abstract
There is now strong evidence to show that the presence of the cellular prion protein (PrP(C)) mediates amyloid-? (A?) neurotoxicity in Alzheimer's disease (AD). Here, we probe the molecular details of the interaction between PrP(C)...
nmrlearner
Journal club
0
02-03-2013 10:19 AM
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Expression and purification of (15)N- and (13)C-isotope labeled 40-residue human Alzheimer's ?-amyloid peptide for NMR-based structural analysis.
Protein Expr Purif. 2011 May 27;
Authors: Long F, Cho W, Ishii Y
Amyloid fibrils of Alzheimer's ?-amyloid peptide (A?) are a primary component of amyloid plaques, a hallmark of Alzheimer's disease (AD). Enormous attention has been given to the structural...
nmrlearner
Journal club
0
06-07-2011 11:05 AM
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Molecular-Level Examination of Cu2+ Binding Structure for Amyloid Fibrils of 40-Residue Alzheimer’s ? by Solid-State NMR Spectroscopy
Sudhakar Parthasarathy, Fei Long, Yifat Miller, Yiling Xiao, Dan McElheny, Kent Thurber, Buyong Ma, Ruth Nussinov and Yoshitaka Ishii
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja1072178/aop/images/medium/ja-2010-072178_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/ja1072178
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA ...
nmrlearner
Journal club
0
02-22-2011 11:06 PM
[NMR paper] Backbone dynamics of a bacterially expressed peptide from the receptor binding domain
Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
Related Articles Backbone dynamics of a bacterially expressed peptide from the receptor binding domain of Pseudomonas aeruginosa pilin strain PAK from heteronuclear 1H-15N NMR spectroscopy.
J Biomol NMR. 2000 Jul;17(3):239-55
Authors: Campbell AP, Spyracopoulos L, Irvin RT, Sykes BD
The backbone dynamics of a 15N-labeled recombinant PAK pilin peptide spanning residues...