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. 2018 Feb 16;8:3212. doi: 10.1038/s41598-018-20811-5

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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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Attributes of AD-114 variants. AD-114 variants were expressed as heterologous proteins in Escherichia coli or Pichia pastoris. The molecular weight of i-body variants was determined by mass spectrometry, binding kinetics were determined by SPR, T_1/2 and T_last values were obtained from in vivo murine pharmacokinetic studies by non-compartmental analysis of the mean plasma concentration of various i-bodies, N = 3 mice per group. (A). Various conjugates were added at the C-terminus of AD-114 (blue) to improve solubility (Im7, red) and circulating half-life (PA600, zig zag). Purification tags were His₆ hexapeptide (orange) and FLAG (purple) (B). Kinetic data set collected for AD-114-PA600-6H binding to immobilized human CXCR4 lipoparticles. Injected i-body concentrations were 160, 80, 40, 20, 10, 5, and 2.5 nM. Data are shown in black and fits to single site kinetic model with mass transport are shown in orange (C). In vivo pharmacokinetic data from mice showing decrease in the plasma concentration of various i-bodies over time, N = 3, error bars show S.E. (D).