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Kinetic and structural analysis of the irreversible inhibition of human monoamine oxidases by ASS234, a multi-target compound designed for use in Alzheimer's disease

AuthorsEsteban, Gerard; Allan, Jennifer; Samadi, Abdelouahid ; Mattevi, Andrea; Unzeta, Mercedes; Marco-Contelles, José ; Binda, Claudia; Ramsay, Rona R.
KeywordsMulti-target drug
Flavin adduct
Alzheimer’s disease
Crystal structure
Issue Date2014
CitationBiochimica et Biophysica Acta - Proteins and Proteomics 1844: 1104- 1110 (2014)
AbstractMonoamine oxidases (MAO) and cholinesterases are validated targets in the design of drugs for the treatment of Alzheimer's disease. The multi-target compound N-((5-(3-(1-benzylpiperidin-4-yl)propoxy)-1-methyl-1H-indol-2-yl) methyl)-N-methylprop-2-yn-1-amine (ASS234), bearing the MAO-inhibiting propargyl group attached to a donepezil moiety that inhibits cholinesterases, retained activity against human acetyl- and butyryl-cholinesterases. The inhibition of MAO A and MAO B by ASS234 was characterized and compared to other known MAO inhibitors. ASS234 was almost as effective as clorgyline (kinact/ KI = 3 × 106 min- 1 M- 1) and was shown by structural studies to form the same N5 covalent adduct with the FAD cofactor.
Identifiersdoi: 10.1016/j.bbapap.2014.03.006
issn: 1878-1454
Appears in Collections:(IQOG) Artículos
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