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. 2024 Mar 20;17(3):398. doi: 10.3390/ph17030398

Figure 8.

Figure 8

Human lactoferricin structure. (a) Lfcin isolated from the crystal structure of hLf. N1 and N2 domains of hLf are represented in blue and lavender respectively, Lfcin structure is represented in yellow. The Trp side chains are highlighted in green in the zoomed-in inset. (b) Ribbon representation of the average energy-minimized structure of hLfcin in aqueous solvent. The structural calculations of hLfcin in aqueous solution indicated a well-defined structure for regions of the peptide. These regions primarily involved Ser6 to Val12, Thr18 to Gln24, and Pro33 to Ile38. This structure shows a helical region for Pro15 to Thr18, and the coiled backbone continues to Gln24. A turn at Lys29 and Val30 leads Val30 to Cys37 back in an anti-parallel alignment to Cys20 to Gln24. However, except for the disulfide bridge from Cys10 to Cys47, there is no close association between Gly1 to Lys19 and Ile38 to Ala49 (figure adapted from [140], PDB: 1Z6W). Image created with PyMOL Molecular Graphic System version 3.0 Schrödinger, LLC.