tailieunhanh - Báo cáo khoa học: Inhibition of a-synuclein fibrillization by dopamine analogs via reaction with the amino groups of a-synuclein Implication for dopaminergic neurodegeneration

Fibrillization ofa-synuclein (a-Syn) is closely associated with the formation of Lewy bodies in neurons and dopamine (DA) is a potent inhibitor for the process, which is implicated in the causative pathogenesis of Parkin-son’s disease (PD). To elucidate any molecular mechanism that may have biological relevance, we tested the inhibitory abilities of DA and several analogs including chemically synthetic and natural polyphenols in vitro. | ềFEBS Journal Inhibition of a-synuclein fibrillization by dopamine analogs via reaction with the amino groups of a-synuclein Implication for dopaminergic neurodegeneration Hong-Tao Li1 Dong-Hai Lin2 Xiao-Ying Luo1 Feng Zhang3 Li-Na Ji1 3 Hai-Ning Du1 Guo-Qiang Song2 Jun Hu3 4 Jia-Wei Zhou1 and Hong-Yu Hu1 1 Key Laboratory of Proteomics Institute of Biochemistry and CellBiology Shanghai Institutes for BiologicalSciences Chinese Academy of Sciences Shanghai China 2 Shanghai Institute of Materia Medica Shanghai China 3 Shanghai Institute of Nuclear Research Shanghai China 4 Bio-X Research Center Shanghai Jiaotong University Shanghai China Keywords a-synuclein dopamine inhibition fibrillization Parkinson s disease Correspondence . Hu Institute of Biochemistry and Cell Biology Shanghai Institutes for Biological Sciences Chinese Academy of Sciences 320 Yue-yang Road Shanghai 200031 P. R. China Fax 86 021 54921011 Tel 86 021 54921121 E-mail hyhu@ Received 28 March 2005 revised 20 May 2005 accepted 25 May 2005 doi Fibrillization of a-synuclein a-Syn is closely associated with the formation of Lewy bodies in neurons and dopamine DA is a potent inhibitor for the process which is implicated in the causative pathogenesis of Parkinson s disease PD . To elucidate any molecular mechanism that may have biological relevance we tested the inhibitory abilities of DA and several analogs including chemically synthetic and natural polyphenols in vitro. The MS and NMR characterizations strongly demonstrate that DA and its analogs inhibit a-Syn fibrillization by a mechanism where the oxidation products quinones of DA analogs react with the amino groups of a-Syn chain generating a-Syn-quinone adducts. It is likely that the amino groups of a-Syn undergo nucleophilic attack on the quinone moiety of DA analogs to form imino bonds. The covalently cross-linked a-Syn adducts by DA are primarily large molecular mass oligomers while those by catechol

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