@article {2017|2040,
	title = {Small static electric field strength promotes aggregation-prone structures in amyloid-β(29-42).},
	journal = {J Chem Phys},
	volume = {146},
	year = {2017},
	month = {2017 Apr 14},
	pages = {145101},
	abstract = {<p>The formation of senile plaques in central neural system resulting from the aggregation of the amyloid β (Aβ) of 40 and 42 residues is one of the two hallmarks of Alzheimer\&$\#$39;s disease. Numerous experiments and computational studies have shown that the aggregation of Aβ peptides in vitro is very complex and depends on many factors such as pH, agitation, temperature, and peptide concentration. The impact of a static electric field (EF) on amyloid peptide aggregation has been much less studied, although EFs may have some applications to treat Parkinson\&$\#$39;s disease symptoms. Here, we study the influence of an EF strength of 20 mV/nm, present in the human brains, on the conformation of the Aβdimer. Our 7 μs non-equilibrium atomistic simulations in aqueous solution show that this field-strength promotes substantially the formation of β-hairpins, believed to be a very important intermediate state during aggregation. This work also suggests that structural biology experiments conducted under appropriate EF strengths may help reduce the conformational heterogeneity of Aβ/Aβdimers and provide significant insights into their structures that may be disease-causing.</p>
},
	issn = {1089-7690},
	doi = {10.1063/1.4979866},
	author = {Lu, Yan and Shi, Xiao-Feng and Salsbury, Freddie R and Philippe Derreumaux}
}
@article {2012|1886,
	title = {Structural, thermodynamical, and dynamical properties of oligomers formed by the amyloid NNQQ peptide: Insights from coarse-grained simulations},
	journal = {J. Chem. Phys.},
	volume = {137},
	number = {2},
	year = {2012},
	month = {jul},
	pages = {025101},
	doi = {10.1063/1.4732761},
	author = {Lu, Yan and Wei, Guanghong and Philippe Derreumaux}
}
@article {2009|2009,
	title = {Structural diversity of the soluble trimers of the human amylin(20-29) peptide revealed by molecular dynamics simulations},
	journal = {J. Chem. Phys.},
	volume = {130},
	number = {12},
	year = {2009},
	month = {mar},
	pages = {125101},
	keywords = {Amino Acid Sequence, Amyloid, Humans, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Multimerization, Protein Structure, Quaternary, Solubility, Solvents},
	doi = {10.1063/1.3097982},
	author = {Mo, Yuxiang and Lu, Yan and Wei, Guanghong and Philippe Derreumaux}
}
