Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B.
A facile synthetic route to substituted trans-2-arylcyclopropylamines was developed to provide access to mechanism-based inhibitors of the human flavoenzyme oxidase lysine-specific histone demethylase LSD1 and related enzyme family members such as monoamine oxidases A and B.
Gooden
David M
DM
Department of Chemistry, Duke University, Durham, NC 27708, USA.
Schmidt
Dawn M Z
DM
Pollock
Julie A
JA
Kabadi
Ami M
AM
McCafferty
Dewey G
DG
D001665:Binding Sites / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D056466:Histone Demethylases; D006657:Histones / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D015394:Molecular Structure; D008995:Monoamine Oxidase / Q000737:chemistry / Q000187:drug effects*; D010089:Oxidoreductases, N-Demethylating / Q000037:antagonists & inhibitors* / Q000737:chemistry; D013329:Structure-Activity Relationship; D014191:Tranylcypromine / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000494:pharmacology
D004791:Enzyme Inhibitors; D006657:Histones; D014191:Tranylcypromine; D056466:Histone Demethylases; D008995:Monoamine Oxidase; C495195:KDM1A protein, human; D010089:Oxidoreductases, N-Demethylating