title: Design of chemical shift-switching 19F magnetic resonance imaging probe for specific detection of human monoamine oxidase A.
abstract: Monoamine oxidase (MAO) A is a flavoenzyme that catalyzes the oxidation of biologically important monoamines and is thought to be associated with psychiatric disorders. Here, we report a strategy for rationally designing a (19)F magnetic resonance imaging probe for the specific detection of human MAO-A (hMAO-A) activity. Our designed (19)F probe was oxidized expeditiously by hMAO-A to produce 2-fluoro-4-nitrophenol via a spontaneous β-elimination mechanism. Concomitant with the structural change of the probe to the product, the (19)F chemical shift changed by 4.2 ppm, which was enough to visualize the probe and enzymatic product separately. Importantly, our probe achieved excellent discrimination of hMAO-A from its isoform hMAO-B.
authors.affiliation: INAMORI Frontier Research Center, Kyushu University, 744 Motooka, Nishi-ku, Fukuoka 819-0395, Japan.
authors.forename: Koya
authors.initials: K
authors.lastname: Yamaguchi
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Ueki
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Nonaka
authors.forename: Fuminori
authors.initials: F
authors.lastname: Sugihara
authors.forename: Tetsuya
authors.initials: T
authors.lastname: Matsuda
authors.forename: Shinsuke
authors.initials: S
authors.lastname: Sando
mesh_terms: D005462:Fluorine Radioisotopes / Q000737:chemistry; D006801:Humans; D008279:Magnetic Resonance Imaging / Q000379:methods*; D015335:Molecular Probes / Q000737:chemistry*; D008995:Monoamine Oxidase / Q000032:analysis* / Q000737:chemistry; D009596:Nitrophenols / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D005462:Fluorine Radioisotopes; D015335:Molecular Probes; D009596:Nitrophenols; C088999:2-fluoro-4-nitrophenol; D008995:Monoamine Oxidase