Fig. 2

Structure prediction of the precursor GIFT-Hep. a The PyMOL predicted structure of the mature region showing antiparallel β-sheets with the characteristic disulfide bonds (C⁷¹–C⁸⁸, C⁷⁴–C⁸⁷, C⁷⁵–C⁸⁴, and C⁷⁷–C⁷⁸) connecting the eight cysteines. The four S–S bonds are numbered, with the fourth one being a vicinal bond located in the hairpin loop. b The Mobyle predicted secondary structure displays the α-helical N-terminal signal peptide region, followed by a random propeptide region and the C-terminal β-sheet region. c The PSIPRED chart illustrates the helix, strand, and coiled regions in the peptide. d The amino acid types comprising the precursor GIFT-Hep, as predicted by the PSIPRED workbench. e The InterPro domain scan server predicted the peptide’s characteristics, identifying it as belonging to the hepcidin family in InterPro, Pfam, and Panther databases. A transmembrane helical region, non-cytoplasmic domain, and the signal peptide helix and coil region were also identified