中文摘要：

目的：研究在大肠杆菌中能够有效抑制α-synuclein异常折叠的小肽，在人神经母细胞瘤SH—SY5Y中的抑制作用。方法：基于α-Syn疏水区域设计的5种透膜小肽在大肠杆菌中能够有效抑制α-synuclein异常折叠；构建真核表达质粒CMV—SynGFP—IRES—Pn并转入SH—SY5Y细胞，通过测定细胞荧光强度分析小肽抑制伐一synuclein异常折叠情况，由此评价大肠杆菌筛选系统确定的小肽在真核SH—SY5Y细胞中的有效性。结果：在大肠杆菌中能有效抑制α-Syn（129A）异常折叠的三种小肽R7P1、R7P3、R7P4，在SH—SY5Y中的作用效果也十分明显，分别比对照肽ASllD提高了114％、98％和98％。对于仪一Syn（53T），R7P1和R7P2在SH—SY5Y中分别比对照提高了90％和44％；然而在两种细胞中，5种透膜小肽对野生型α-Syn（wr）的作用与对照相比差距不明显。

英文摘要：

Objective： Small peptides screened from E. coli can inhibit the abnormal α- synuclein aggregation in neuroblastoma SH - SY5Y cells. Method： Five membrane permeational peptides RTP1 - R7P5 were designed based on hydrophobic regions; Eukaryotic expression vector CMV -SynGFP-IRES-Pn were transfected into SH -SY5Y cell,the inhibition of α-synuclein from abnormal aggregation of the small peptide was measured by cell fluorescence strength, to evaluate the effectiveness of E. coli screening system. Result： The small peptides （ RTPI , RTP3, RTP4） can inhibit α- Syn （S129A） abnormal folding in E. coli, also have significant effect in SH - SY5Y. Compared with ASI1D, R7P1, R7P3, R7P4 were 114% ,98% and 98% more effective in inhibiting abnormal aggregation of α- Syn （S129A） respectively. RTP1 and R7P2 were 90% and 44% more effective in inhibiting abnormal an＆negation of α- Syn （A53T） respectively. However, the difference between the effectiveness of five small peptides and ASI1D for the wildtype α-Syn （WT） is not obvious.