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. 2019 Jan 11;9:59. doi: 10.1038/s41598-018-37276-1

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Probable role of α-strand in the aggregation of α-synuclein. (A) Suggested stages of aggregation process. N-terminus, NAC region and C-terminus are highlighted in blue, green and pink, respectively. Biophysical studies have confirmed that isolated α-synuclein monomer is intrinsically disordered in vitro and aggregation results in the formation of amyloid fibrils. Occasionally, region 72–74 of α-synuclein monomer adopts an α-strand conformation. The α-strands of α-synuclein oligomers interact through hydrogen bonding to form α-sheet structure. Subsequently, α-sheet acts as a possible nucleus that initiate aggregation and fibrillation of α-synuclein. (B) A model for α-sheet intermediate where partial charges on the interface are indicated by red (negative charges) and blue (positive charges) colors.