Notice of RetractionScreen alpha-Synuclein Aggregation Inhibitor Short Peptides with GFP Coexpression Fusion System

Notice of Retraction

After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE´s Publication Principles.

We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.

The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.

The aggregation of α-synuclein (a-Syn) is implicated as a critical factor in Parkinson´s disease and other neurodegenerative diseases. Some short peptides based on the native sequences of amyloid proteins are able to prevent the β sheet-rich aggregation and block the toxicity of the aggregates. In this study, five kind short peptides with delivery peptide R7P1~R7P5 were designed, and α-syn(A53T), a-syn(S129A) and α-Syn(WT) which are mutants of α-syn were used as research objects. Fused α-Syn protein domain upstream to Green Fluorescence Protein (GFP), and bicistronic coexpressed the short peptides with delivery system with α-Syn to form a GFP coexpression fusion system. The corresponding correct expressed clones were obtained in E.Coli. GFP was used as label to make the fold of protein visible. The changes of the fold states of these three mutants caused by the action of the designed short peptides were observed. Results showed that, for α-Syn (A53T) G, α Syn(S129A)G and α-Syn(WT)G, the inhibition aggregation ability of short peptide R7P3 (M(R)7KLMRVGGA VVTGR) increased 43%, 140%, and 117% with ASH (MGGAVVTGR) as control, and increased 47% 64% and 39% with ASI1D (MRRGGAVVTG(R)6) as control. At the same time, for the inhibition aggregation of α-Syn(A53T)G and α-Syn(S129A)G, R7P3 increased 16% and 95% higher than those of without delivery system P3 respectively. Therefore, R7P3 (M(R)7 KLMRVGGAVVTGR) is a promising short- peptide with delivery system for the inhibition aggregation of α-Syn G.