Affiliations: [a] Laboratoire de Biochimie Théorique, UPR 9080 CNRS, Université Paris Diderot, Sorbonne Paris Cité, IBPC, Paris, France
| [b] Manchester Institute of Biotechnology and Department of Chemistry, Faculty of Science and Engineering, The University of Manchester, Manchester, UK
| [c] CNRS, LCC (Laboratoire de Chimie de Coordination), Toulouse Cedex 4, France et Université de Toulouse, UPS, INPT, Toulouse Cedex 4, France
| [d] Biometals and Biology Chemistry, Institut de Chimie (CNRS UMR7177), Université de Strasbourg, Strasbourg, France
Correspondence:
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Correspondence to: Philippe Derreumaux, Laboratoire de Biochimie Théorique, UPR 9080 CNRS, Université Paris Diderot, Sorbonne Paris Cité, IBPC, 13 rue Pierre et Marie Curie, 75005, Paris, France. E-mail: philippe.derreumaux@ibpc.fr.
Abstract: Targeting the early oligomers formed by the amyloid-β (Aβ) peptide of 40 and 42 amino acids is considered one promising therapeutic approach for Alzheimer’s disease (AD). In vitro experiments and computer simulations are often used in synergy to reveal the modes of interactions of drugs. In this account, we present our contribution to understanding how small molecules bind to Aβ40/Aβ42 peptides, based either on extensive coarse-grained and all-atom simulations, or a variety of experimental techniques. We conclude by offering several perspectives on the future of this field to design more efficient drugs.
