@article{kaffy_brinet_soulier_correia_tonali_fera_iacone_hoffmann_khemtémourian_crousse_et al., 
  title={Designed glycopeptidomimetics disrupt protein-protein interactions mediating amyloid β-peptide aggregation and restore neuroblastoma cell viability ACS Paragon Plus Environment Journal of Medicinal Chemistry Designed glycopeptidomimetics disrupt protein-protein interactions mediating amyloid β-peptide aggregation and restore neuroblastoma cell viability}, 
  abstractNote={How anti-Alzheimer's drug candidates that reduce amyloid 1-42 peptide fibrillization interact with the most neurotoxic species is far from being understood. We report herein the capacity of sugar-based peptidomimetics to inhibit both Aβ 1-42 early oligomerization and fibrillization. A wide range of bio-and physico-chemical techniques, such as a new capillary electrophoresis method, nuclear magnetic resonance, and surface plasmon resonance, were used to identify how these new molecules can delay the aggregation of Aβ 1-42. We demonstrate that these molecules interact with soluble oligomers in order to maintain the presence of non-toxic monomers and to prevent fibrillization. These compounds totally suppress the toxicity of Aβ 1-42 towards SH-SY5Y neuroblastoma cells, even at sub-stoichiometric concentrations. Furthermore, demonstration that the best molecule combines hydrophobic moieties, hydrogen bond donors and acceptors, ammonium groups and a hydrophilic β-sheet breaker element, provides valuable insight for the future structure-based design of inhibitors of Aβ 1-42 aggregation.}, 
  author={Kaffy and Brinet and Soulier and Correia and Tonali and Fera and Iacone and Hoffmann and Khemtémourian and Crousse and et al.}
  }