Kim Jisook, Lee Irene N
Department of Chemistry and Physics, University of Tennessee at Chattanooga, Chattanooga, TN 37403, USA.
Department of Chemistry, Case Western Reserve University, Cleveland, OH 44106, USA.
Bioorg Chem. 2017 Dec;75:265-273. doi: 10.1016/j.bioorg.2017.10.007. Epub 2017 Oct 16.
In this paper, we report the inactivation of copper containing bovine plasma amine oxidase (BPAO) by a series of saturated alkylamines containing halogen atoms at γ-position, which are 1,1,1-trihalo-3-aminopropane, 1,1,1-trifluoro-2-hydroxy-3-aminopropane, 1,1,1-trichloro-2-hydroxy-3-aminopropane, and 1,1,1-trichloro-2-(2-phenethyloxy)-3-aminopropane. The trihalo-2-hydroxypropylamine analogs exhibited a time-dependent inactivation behavior of BPAO, with 1,1,1-trifluoro-2-hydroxy-3-aminopropane as the most efficient inactivator. The incorporation of a OH group at β-position increased inactivation efficiency by 10-fold within the trifluoro analogs, and the incorporation of a phenethyloxy group at β-position exhibited a higher efficiency by 3-fold within the trichloro analogs based on I values. All four compounds were found to be irreversible inactivators for BPAO.
