Rusfertide is a synthetic peptide containing aliphatic, aromatic, and charged residues that produce varied secondary-structure motifs. Researchers examine it to evaluate peptide-receptor interactions, conformational flexibility, and solvent-driven behavior. Its functional arrangement supports mechanistic and structural exploration.
CAT No: R2421
CAS No:1628323-80-7
Synonyms/Alias:Rusfertide;Rusfertide [USAN];XM71MYX0IQ;PTG-300FB;PTG-300;UNII-XM71MYX0IQ;RUSFERTIDE [INN];1628323-80-7;WHO 11456;Isovaleryl-Asp-Thr-His-Phe-Pro-cyclo(Cys-Ile-Lys(palm-gamma-Glu)- Phe-Glu-Pro-Arg-Ser-Lys-Gly-Cys)-Lys-NH2;L-LYSINAMIDE, N-(3-METHYL-1-OXOBUTYL)-L-.ALPHA.-ASPARTYL-L-THREONYL-L-HISTIDYL-L-PHENYLALANYL-L-PROLYL-L-CYSTEINYL-L-ISOLEUCYL-N6-(N-(1-OXOHEXADECYL)-L-.GAMMA.-GLUTAMYL)-L-LYSYL-L-PHENYLALANYL-L-.ALPHA.-GLUTAMYL-L-PROLYL-L-ARGINYL-L-SERYL-L-LYSYLGLYCYL-L-CYSTEINYL-;N-(3-METHYL-1-OXOBUTYL)-L-.ALPHA.-ASPARTYL-L-THREONYL-L-HISTIDYL-L-PHENYLALANYL-L-PROLYL-L-CYSTEINYL-L-ISOLEUCYL-N6-(N-(1-OXOHEXADECYL)-L-.GAMMA.-GLUTAMYL)-L-LYSYL-L-PHENYLALANYL-L-.ALPHA.-GLUTAMYL-L-PROLYL-L-ARGINYL-L-SERYL-L-LYSYLGLYCYL-L-CYSTEINYL-L-LYSINAMIDE;Hepcidin Agonist PTG-300;Hepcidin Mimetic PTG-300;PTG300;PTG 300;ISOVALERYL-ASP-THR-HIS-PHE-PRO-CYCLO(CYS-ILE-LYS(PALM-GAMMA-GLU)-PHE-GLU-PRO-ARG-SER-LYS-GLY-CYS)-LYS-NH2;L-LYSINAMIDE, N-(3-METHYL-1-OXOBUTYL)-L-ALPHA-ASPARTYL-L-THREONYL-L-HISTIDYL-L-PHENYLALANYL-L-PROLYL-L-CYSTEINYL-L-ISOLEUCYL-N6-(N-(1-OXOHEXADECYL)-L-GAMMA-GLUTAMYL)-L-LYSYL-L-PHENYLALANYL-L-ALPHA-GLUTAMYL-L-PROLYL-L-ARGINYL-L-SERYL-L-LYSYLGLYCYL-L-CYSTEINYL-;L-Lysinamide, N-(3-methyl-1-oxobutyl)-L-alpha-aspartyl-L-threonyl-L-histidyl-L-phenylalanyl-L-prolyl-L-cysteinyl-L-isoleucyl-N6-[N-(1-oxohexadecyl)-L-gamma-glutamyl]-L-lysyl-L-phenylalanyl-L-alpha-glutamyl-L-prolyl-L-arginyl-L-seryl-L-lysylglycyl-L-cysteinyl-, cyclic (6-->16)-disulfide;N-(3-METHYL-1-OXOBUTYL)-L-ALPHA-ASPARTYL-L-THREONYL-L-HISTIDYL-L-PHENYLALANYL-L-PROLYL-L-CYSTEINYL-L-ISOLEUCYL-N6-(N-(1-OXOHEXADECYL)-L-GAMMA-GLUTAMYL)-L-LYSYL-L-PHENYLALANYL-L-ALPHA-GLUTAMYL-L-PROLYL-L-ARGINYL-L-SERYL-L-LYSYLGLYCYL-L-CYSTEINYL-L-LYSINAMIDE;
Rusfertide is a synthetic peptide compound designed to mimic the biological activity of natural hepcidin, a key regulator of systemic iron homeostasis. As a hepcidin mimetic, it exhibits a high affinity for ferroportin, the principal iron exporter in mammalian cells, thereby modulating iron absorption and distribution within the body. The unique structure and functional properties of Rusfertide have made it an important tool for researchers investigating the molecular mechanisms of iron metabolism, iron overload disorders, and related regulatory pathways. Its stability and specificity also position it as a valuable asset in studies focused on peptide-based modulation of metal ion transport and homeostatic control.
Iron Metabolism Research: Rusfertide is extensively utilized in biochemical and molecular biology laboratories to elucidate the regulatory pathways governing iron homeostasis. By acting as a surrogate for endogenous hepcidin, it enables detailed investigation of ferroportin-mediated iron export from enterocytes, macrophages, and hepatocytes. Researchers employ this peptide to model iron sequestration and release in vitro, helping to clarify the role of hepcidin-analogues in iron sensing and systemic iron balance. Such studies are critical for advancing the understanding of iron overload and deficiency states at the cellular and organismal levels.
Peptide Mechanism of Action Studies: The compound serves as a robust model for examining the structure-activity relationships of hepcidin-like peptides. Its defined sequence and bioactivity allow scientists to dissect the molecular interactions between hepcidin analogues and ferroportin, facilitating the mapping of critical binding domains and conformational changes necessary for iron regulation. This application is particularly valuable for designing next-generation peptide mimetics with tailored biological effects, as well as for exploring the broader implications of peptide-protein interactions in metal ion transport.
Drug Discovery and Preclinical Screening: In pharmaceutical research and development, Rusfertide is employed as a reference compound in high-throughput screening assays and preclinical models focused on iron regulatory pathways. Its well-characterized activity profile supports the evaluation of novel small molecules, peptides, or biologics intended to modulate iron metabolism. By serving as a benchmark or control, it enables comparative analyses that inform lead optimization and structure-guided drug design targeting iron homeostasis.
Analytical Method Development: The peptide's defined chemical structure and biological activity make it suitable for use as a standard or calibrator in analytical assays designed to quantify hepcidin activity or ferroportin modulation. Laboratories leverage Rusfertide in the validation of bioanalytical methods, such as mass spectrometry-based quantification or immunoassays, to ensure accuracy and reproducibility in the measurement of peptide-mediated iron regulation. This aids in the development of robust assays for both basic research and industrial applications.
Biochemical Pathway Elucidation: Researchers investigating the broader network of proteins and signaling molecules involved in iron metabolism utilize Rusfertide to perturb specific nodes within these pathways. By introducing the peptide into cellular or animal models, scientists can observe downstream effects on gene expression, protein localization, and iron distribution, thereby unraveling complex regulatory circuits. Such studies contribute to a systems-level understanding of iron homeostasis and inform the identification of novel biomarkers or therapeutic targets for iron-related disorders.
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