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. 2019 Apr 5;9:5715. doi: 10.1038/s41598-019-41993-6

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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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Stability of RD2 and l-RD2 in SGF, SIF, human plasma and human liver microsomes. RD2 and l-RD2 were incubated in SGF, SIF, human plasma and human liver microsomes. In SGF (A) and SIF (B), RD2 remained stable for 24 h. In contrast, l-RD2 was degraded by 23 ± 4% within the same time in SGF and was even completely metabolized within a few seconds in SIF. Human plasma (C) and human liver microsomes (D) metabolized l-RD2 several hundred times faster than RD2. Peak areas of the unmetabolized peptides after different incubation times were normalized to the peptides’ peak areas after direct extraction from the media. Data are presented as mean ± SD (n = 3).