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. 2019 Jul 23;9:10636. doi: 10.1038/s41598-019-47011-z

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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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Infrared microscopy analysis. (A) Analytical area on the peptide film. Visual fields for recording the infrared spectra around the irradiated spot (red circle) were shown as yellow squares (100•100 μm). For the peptide fibril before irradiation (Non-irradiation fibril), a representative area was shown. (B) Averaged spectra at mid-infrared region (left) and at near-infrared region (right). Infrared spectrum before fibrillation (Pre-fibril) was obtained as single spectrum in the transmission mode by using potassium bromide pellet. (C) Conformational analysis. The proportion of each conformation (α-Helix [triangle], β-Sheet [black circle], β-Turn [cross], and other conformation [diamond]) was obtained based on the intensity at amide I band in the averaged spectrum (B).