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. 2018 Aug 23;8:12700. doi: 10.1038/s41598-018-31058-5

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© The Author(s) 2018

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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ATR-FTIR analysis of the amino acid functionalized ns-nHA NH₂-H⁺ peak area normalized to PO₄³⁻ peak area. Lysine-functionalized ns-nHA was found to have the greatest symmetric NH₂-H⁺ peak area. However, there are two NH₂-H⁺ groups per lysine molecule (aspartic acid and glycine only have one NH₂-H⁺ group per molecule). As shown by the white horizontal dashed line on the lysine column, the NH₂-H⁺ peak area analysis suggests that there is a comparable amount of lysine attached to the ns-nHA surface as glycine. Data reported as average ± one standard deviation (n = 3). ns-nHA unsaturated with calcium is given as US, while that pre-saturated with calcium is given as CaS. Horizontal bars indicate statistically detectable difference (p < 0.05).