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. 2019 Feb 21;9:2530. doi: 10.1038/s41598-018-38401-w

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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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Oligomer formation in wild type and the ala-scanned peptides. (A) Snapshot of the initial (1 ns) and later stages (Wild (90.11 ns), N1A (99.30 ns), F2A (79.26 ns), G3A (86.98 ns), I5A (90.63 ns), L6A (88.62 ns), S7A (87.25 ns) and S8A (81.22 ns) peptide clusters- clusters are shown by ribbon models where coil, helices, and sheets are shown in ‘grey’, ‘yellow’ and ‘blue’, respectively) configuration. The ‘initial structure’ shows wild type snapshot at 1 ns which was similar for all the mutants. Initially, 27 peptides were aligned parallelly inside a cubic box [(104 Ǻ)³] with approximately 30,000 water molecules which form oligomers during the simulation. These structures were rendered using Rastop (Valadon P., www.geneinfinity.org/rastop/). (B) Time dependence of the mean cluster size (MCS). MCS is plotted against time for all the eight systems. Large clusters were observed for all the analogs by the end of the simulation.