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. 2021 Jan 29;11:2629. doi: 10.1038/s41598-021-81905-1

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Analytical characterization of Samples 1–6. Relative abundance of Lys residues obtained by peptide mapping of free amino acids in RNase A conjugated with different scaffolds: glyoxyl-agarose (sample 1), CDI-agarose (sample 2), GPTS-agarose (sample 3), glutaraldehyde-agarose (sample 4), APTS-glutaraldehyde-agarose (sample 5) and CNBr-agarose (sample 6). Colors indicate the percentage abundance of each Lys residue normalized respect to the most abundant peptide in the corresponding analysis. The following legend was used: red 0–20%; orange 20–40%; yellow 40–60%; green 60–100%. Consequently, red = Lys bound to the carrier; green = Lys exposed on the surface, not involved in the binding. Created with PyMOL Molecular Graphics System (version 1.1 eval, http://www.pymol.org).