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. 2013 Aug 20;21(12):2236–2246. doi: 10.1038/mt.2013.178

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Copyright © 2013 The American Society of Gene & Cell Therapy

This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 3.0 License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/3.0/

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Characterization and postselection optimization of C5a-binding Spiegelmer. SPR measurement of NOX-D19 binding to (a) mouse and (b) human C5a. Kinetic rate constants k_a and k_d are shown as mean ± SEM. Data are representative for at least 3 individual measurements. (c) Kinetic rate constants of 2′-deoxyribonucleotide-modified NOX-D19001 variants binding to huC5a were determined by SPR measurement. For unmodified NOX-D19001 (black diamond; dotted lines) mean ± SD of 5 injections is shown. Six modified variants of NOX-D19001 (D09, D16, D17, D30, D32, and D40) with increased overall affinity (K_d = k_d/k_a) were chosen and combined to the six-times modified Spiegelmer NOX-D19001-6xDNA (black square). (d) Inhibition by NOX-D19 (black diamonds) and NOX-D20 (black squares) of CD88⁺ BA/F3 cell chemotaxis stimulated with 0.1 nmol/l huC5a. Mean ± SD of triplicate measurements is shown. Data are representative for four independent experiments. RU, response units.