@article {2017|2032,
	title = {Conformational Ensembles of the Wild-Type and S8C Aβ1-42 Dimers.},
	journal = {J Phys Chem B},
	volume = {121},
	year = {2017},
	month = {2017 Mar 23},
	pages = {2434-2442},
	abstract = {<p>We characterized the dimer of the amyloid-β wild-type (WT) peptide, Aβ, of 42 residues and its disulfide-bond-locked double mutant (S8C) by replica exchange molecular dynamics simulations. Aβ dimers are known to be the smallest toxic species in Alzheimer\&$\#$39;s disease, and the S8C mutant has been shown experimentally to form an exclusive homogeneous and neurotoxic dimer. Our 50 μs all-atom simulations reveal similar secondary structures and collision cross-sections but very different intramolecular and intermolecular conformations upon double S8C mutation. Both dimers are very dynamic with hundreds of free-energy minima that differ from the U-shape and S-shape conformations of the peptides in the fibrils. The only common structural feature, shared by both species with a probability of 4\% in WT and 12\% in S8C-S8C, is a three-stranded β-sheet spanning the 17-23, 29-36, and 39-41 residues, which does not exist in the Aβ40 WT dimers.</p>
},
	issn = {1520-5207},
	doi = {10.1021/acs.jpcb.7b00267},
	author = {Man, Viet Hoang and Phuong Hoang Nguyen and Philippe Derreumaux}
}
