Oueis_2014_Org.Biomol.Chem_12_156

Reference

Title : Reaction site-driven regioselective synthesis of AChE inhibitors - Oueis_2014_Org.Biomol.Chem_12_156
Author(s) : Oueis E , Santoni G , Ronco C , Syzgantseva O , Tognetti V , Joubert L , Romieu A , Weik M , Jean L , Sabot C , Nachon F , Renard PY
Ref : Org Biomol Chem , 12 :156 , 2014
Abstract : The enzyme-directed synthesis is an emerging fragment-based lead discovery approach in which the biological target is able to assemble its own multidentate ligands from a pool of building blocks. Here, we report for the first time the use of the human acetylcholinesterase (AChE) as an enzyme for the design and synthesis of new potent heterodimeric huprine-based inhibitors. Both the specific click chemistry site within the protein and the regioselectivity of the Huisgen cycloaddition observed suggest promising alternatives in the design of efficient mono- and dimeric ligands of AChE. Finally, a detailed computational modelling of the click reaction was conducted to further understand the origin of this TGS selectivity.
ESTHER : Oueis_2014_Org.Biomol.Chem_12_156
PubMedSearch : Oueis_2014_Org.Biomol.Chem_12_156
PubMedID: 24216754

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Citations formats

Oueis E, Santoni G, Ronco C, Syzgantseva O, Tognetti V, Joubert L, Romieu A, Weik M, Jean L, Sabot C, Nachon F, Renard PY (2014)
Reaction site-driven regioselective synthesis of AChE inhibitors
Org Biomol Chem 12 :156

Oueis E, Santoni G, Ronco C, Syzgantseva O, Tognetti V, Joubert L, Romieu A, Weik M, Jean L, Sabot C, Nachon F, Renard PY (2014)
Org Biomol Chem 12 :156