By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Proteins. According to news reporting originating from Shanghai, People's Republic of China, by NewsRx correspondents, research stated, "The formation of an a-synuclein fibril is critical in the pathogenesis of Parkinson's disease. The native unfolded a-synuclein monomer will translocate through an alpha-hemolysin nanopore by applied potential at as physiological conditions in vitro."
Our news editors obtained a quote from the research from Fudan University, "Applying a potential transformed a-synuclein into a partially folded intermediate, which was monitored by capture inside the vestibule of an alpha-hemolysin nanopore with a capture current of 20 +/- 1.0 pA. The procedure involves the critical early stage of alpha-synuclein structural transformation. Further elongation of the intermediate produces a block current to 5 +/- 0.5 pA. It is revealed that the early stage fibril of a-synuclein inside the nanopore is affected by intrapeptide electrostatic interaction. In addition, trehalose cleared the fibrillation by changing the surface hydrophobic interaction of A53T alpha-synuclein, which did not show any inhibition effect from WT alpha-synuclein. The results proved that the interpeptide hydrophobic interactions in the elongation of A53T alpha-synuclein protofilaments can be greatly weakened by trehalose. This suggests that trehalose inhibits the interpeptide interaction involved in protein secondary structure. The hydrophobic and electrostatic interactions are associated with an increase in a-synuclein fibrillation propensity."
According to the news editors, the research concluded: "This work provides unique insights into the earliest steps of the a-synuclein aggregation pathway and provides the potential basis for the development of drugs that can prevent alpha-synuclein aggregation at the initial stage."
For more information on this research see: Analysis of a Single alpha-Synuclein Fibrillation by the Interaction with a Protein Nanopore. Analytical Chemistry, 2013;85(17):8254-8261. Analytical Chemistry can be contacted at: Amer Chemical Soc, 1155 16TH St, NW, Washington, DC 20036, USA. (American Chemical Society - www.acs.org; Analytical Chemistry - www.pubs.acs.org/journal/ancham)
The news editors report that additional information may be obtained by contacting H.Y. Wang, Fudan University, Huashan Hosp, Dept. of Neurol, Shanghai 200040, People's Republic of China. Additional authors for this research include Z. Gu, C. Cao, J. Wang and Y.T. Long (see also Proteins).
Keywords for this news article include: Asia, Shanghai, alpha-Synuclein, Nerve Tissue Proteins, People's Republic of China
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