Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B

David M Gooden; Dawn M Z Schmidt; Julie A Pollock; Ami M Kabadi; Dewey G McCafferty

doi:10.1016/j.bmcl.2008.01.003

Facile synthesis of substituted trans-2-arylcyclopropylamine inhibitors of the human histone demethylase LSD1 and monoamine oxidases A and B

Bioorg Med Chem Lett. 2008 May 15;18(10):3047-51. doi: 10.1016/j.bmcl.2008.01.003. Epub 2008 Jan 8.

Authors

David M Gooden¹, Dawn M Z Schmidt, Julie A Pollock, Ami M Kabadi, Dewey G McCafferty

Affiliation

¹ Department of Chemistry, Duke University, Durham, NC 27708, USA.

Abstract

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.

MeSH terms

Binding Sites / drug effects
Enzyme Inhibitors / chemical synthesis*
Enzyme Inhibitors / chemistry
Enzyme Inhibitors / pharmacology
Histone Demethylases
Histones / chemistry*
Humans
Kinetics
Molecular Structure
Monoamine Oxidase / chemistry
Monoamine Oxidase / drug effects*
Oxidoreductases, N-Demethylating / antagonists & inhibitors*
Oxidoreductases, N-Demethylating / chemistry
Structure-Activity Relationship
Tranylcypromine / analogs & derivatives
Tranylcypromine / chemical synthesis*
Tranylcypromine / pharmacology

Substances

Enzyme Inhibitors
Histones
Tranylcypromine
Histone Demethylases
Monoamine Oxidase
KDM1A protein, human
Oxidoreductases, N-Demethylating

Abstract

MeSH terms

Substances

Grants and funding