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Articles by Mei-sha Chen
Total Records ( 2 ) for Mei-sha Chen
  Xun Sun , Wei-hui Wu , Qian Liu , Mei-sha Chen , Ye-ping Yu , Ying Ma , Yu-fen Zhao and Yan-mei Li

Abnormal assembly of monomeric β-amyloid (Aβ) in Alzheimer's disease leads to the formation of most neurotoxic oligomers in vivo. In this study, we explored a linking strategy to design hybrid peptides, by combining the Aβ recognition motif and the solvent disruptive sequences. We found that in vitro all synthetic peptides with the recognition motif can affect Aβ fibrillization and alter the morphology of Aβ aggregates variously, different from those without the recognition motif. The effects of peptides containing recognition motif on Aβ aggregation correlate with their abilities to change the surface tension of solutions. In addition, compounds with the recognition motif, not those without such motif, can inhibit cytotoxicity of Aβ in cell culture probably by decreasing the amount of toxic Aβ oligomers. These results indicate that recognition domain and solvent effect should be considered as important factors when designing molecules to target Aβ aggregation.

  Wei-hui Wu , Peng Lei , Qian Liu , Jia Hu , Adam P. Gunn , Mei-sha Chen , Yan-fang Rui , Xiao-yang Su , Zuo-ping Xie , Yu-Fen Zhao , Ashley I. Bush and Yan-mei Li
  Decelerated degradation of β-amyloid (Aβ) and its interaction with synaptic copper may be pathogenic in Alzheimer disease. Recently, Co(III)-cyclen tagged to an aromatic recognition motif was shown to degrade Aβ in vitro. Here, we report that apocyclen attached to selective Aβ recognition motifs (KLVFF or curcumin) can capture copper bound to Aβ and use the Cu(II) in place of Co(III) to become proteolytically active. The resultant complexes interfere with Aβ aggregation, degrade Aβ into fragments, preventing H2O2 formation and toxicity in neuronal cell culture. Because Aβ binds Cu in amyloid plaques, apocyclen-tagged targeting molecules may be a promising approach to the selective degradation of Aβ in Alzheimer disease. The principle of copper capture could generalize to other amyloidoses where copper is implicated.
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