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. 2019 Sep 11;9:13147. doi: 10.1038/s41598-019-48299-7

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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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E40 completely removes the immunogenicity of the 33-mer peptide. LC/MS profile of 33-mer digestion by E40 at pH 5 and 37 °C, with E40 in a molar ratio 1:48 versus peptide. Panel (A): Trace of full length peptide alone (triply charged ion [(M + 3 H⁺)³⁺ = 1304.68]). Panels (B–E): Time-course of 33-mer cleavage by E40 activity (from to top-bottom 0, 15, 30, 60 minutes digestion, respectively). Peptide fragments formed during digestion are indicated by arrows. Rapid action of E40 onto the substrate can be visible at time 0′, complete disappearance of 33-mer is obtained already after 15′ of digestion. Panel (F): Schematic visualization of E40 cleavage sites deduced from the final residual peptides which demonstrates the complete epitopes destruction since 30′ reaction.