Yu WY

References (2)

Title : Design, synthesis and biological evaluation of benzylisoquinoline derivatives as multifunctional agents against Alzheimer's disease - Xu_2014_Bioorg.Med.Chem.Lett_24_2368
Author(s) : Xu ZC , Wang XB , Yu WY , Xie SS , Li SY , Kong LY
Ref : Bioorganic & Medicinal Chemistry Lett , 24 :2368 , 2014
Abstract : A novel series of benzylisoquinoline derivatives were designed, synthesized, and evaluated as multifunctional agents against Alzheimer's disease (AD). The screening results showed that most of the compounds significantly inhibited cholinesterases (ChEs), human cholinesterases (h-ChEs) and self-induced beta-amyloid (Abeta) aggregation. In particular, compound 9k showed the strongest acetylcholinesterase (AChE) inhibitory activity, being 1000-fold and 3-fold more potent than its precursor benzylisoquinoline (10) and the positive control galanthamine, respectively. In addition, 9k was a moderately potent inhibitor for h-ChEs. Compared with precursor benzylisoquinoline (36.0% at 20mucapital EM, Cyrillic), 9k (78.4% at 20mucapital EM, Cyrillic) could further inhibit Abeta aggregation. Moreover, 9k showed low cell toxicity in human SH-SY5Y neuroblastoma cells. Therefore, compound 9k might be a promising lead compound for AD treatment.
ESTHER : Xu_2014_Bioorg.Med.Chem.Lett_24_2368
PubMedSearch : Xu_2014_Bioorg.Med.Chem.Lett_24_2368
PubMedID: 24726809

Title : Characteristics of recombinant human butyrylcholinesterase - Yuan_1999_Zhongguo.Yao.Li.Xue.Bao_20_74
Author(s) : Yuan HJ , Yu WY , Shi CH , Sun MJ
Ref : Zhongguo Yao Li Xue Bao , 20 :74 , 1999
Abstract : AIM: To study the biochemical-pharmacological properties of the recombinant human butyrylcholinesterase (rhBChE) and thereby to size up the potential possibility of using it as a detoxifying agent in succinylcholine intoxication.
METHODS: CHO-dhfr cells were transfected with plasmids by electroporation. BChE activity was determined colorimetrically by 5, 5'-dithiobis-(2-nitrobenzoic acid) (DTNB) method. Antigenicity was estimated by enzyme-linked immunosorbent assay and Western blot.
RESULTS: The maximal expression amounted to 25.83 ng.h-1/10(6) cells. The rhBChE was highly similar to the native human BChE (nhBChE) in terms of its catalytic property, substrate affinity, inhibitor sensitivity, reactivation, stability, and immunoreactivity with anti-nhBChE antibodies. Mice challenged with 1.5 lethal dose of succinylcholine preincubated with rhBChE survived without any symptoms of intoxication. CONCLUSION: The rhBChE and nhBChE exhibit similar biochemical-pharmacological features. It is of potential value in practical use.
ESTHER : Yuan_1999_Zhongguo.Yao.Li.Xue.Bao_20_74
PubMedSearch : Yuan_1999_Zhongguo.Yao.Li.Xue.Bao_20_74
PubMedID: 10437130