TY - CONF A1 - Vranic, Marija A1 - Starke, I. A1 - Weller, Michael G. A1 - Möller, H. M. T1 - Metal-binding properties of the cystein-rich biomarker Hepcidin-25 N2 - Hepcidin-25 regulates iron homeostasis in response to inflammation, erythropoietic demand and iron stores. The liver synthesizes three types of hepcidin, only hepcidin-25 indirectly regulates and coordinates use and storage of iron. Hepcidin-25 contains a well defined β-sheet and β-hairpin loop stabilized by four disulfide bonds. The N-terminus which plays a crucial role in the biological activity of hepcidin-25 was found to be disordered. The ATCUN motif sequence is present at the N-terminus (Asp-Thr-His). The ATCUN motif (H2N-X-X-His) binds Cu2+ and Ni2+ with high affinity and always contains histidine in its sequence. NMR provides an ideal tool to determine hepcidin-25’s threedimensional(3D) structure taking into account the Cu2+ and Ni2+ binding capacity of hepcidin’s ATCUN motif. T2 - 3rd International Conference Proteins and Peptides, Structure, Function and Biotechnology CY - Geneva, Switzerland DA - 23.07.2018 KW - Peptides KW - Metalloproteins KW - Chromatography KW - ATCUN KW - Nickel KW - Copper KW - SUMO KW - Fusion protein KW - Iron disorders KW - ESI-MS KW - RP-HPLC PY - 2018 AN - OPUS4-46945 LA - eng AD - Bundesanstalt fuer Materialforschung und -pruefung (BAM), Berlin, Germany ER -