| Target Molecule | Adrenomedullin (AM) (1-52), human |
| Synonyms | Adrenomedullin (AM), human; ADM (1-52), human; Human adrenomedullin-(1-52)-NH2 |
| CAS Number | 148498-78-6 |
| Sequence (3-Letter) | H-Tyr-Arg-Gln-Ser-Met-Asn-Asn-Phe-Gln-Gly-Leu-Arg-Ser-Phe-Gly-Cys-Arg-Phe-Gly-Thr-Cys-Thr-Val-Gln-Lys-Leu-Ala-His-Gln-Ile-Tyr-Gln-Phe-Thr-Asp-Lys-Asp-Lys-Asp-Asn-Val-Ala-Pro-Arg-Ser-Lys-Ile-Ser-Pro-Gln-Gly-Tyr-NH2 (Disulfide bridge: Cys16-Cys21) |
| Sequence (1-Letter) | YRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGY-NH2 |
| Molecular Formula | C₂₆₄H₄₀₆N₈₀O₇₇S₃ |
| Molecular Weight | 6028.8 |
| Service Category | Custom Peptide Synthesis / CDMO Manufacturing |
| Synthesis Purity | Customizable (e.g., ≥95%, ≥98% via HPLC) |
| Appearance | White to off-white lyophilized powder |
| Counter Ion | Acetate, TFA, or custom salt options |
| Synthesis Technology | Solid-Phase Peptide Synthesis (SPPS) and Directed Disulfide Cyclization |
| Modification Options | Intramolecular disulfide cyclization, C-terminal amidation, stable isotope labeling, fluorescent tags |
| Available Scale | Milligram (R&D) to Kilogram (Commercial CDMO) |
| Analytical Data | COA, HPLC, MS, and disulfide connectivity verification provided per batch |
| Usage | Raw material synthesized strictly for laboratory research, analytical development, and industrial formulation. Not a finished medicine. |
Adrenomedullin (1-52), human (CAS 148498-78-6) is a 52-amino acid regulatory peptide characterized by an intramolecular Cys16-Cys21 disulfide bridge and C-terminal amidation. We target this sequence to supply high-purity reference materials, analytical standards, and raw materials for cardiovascular research.
We utilize optimized solid-phase peptide synthesis (SPPS) on specialized amide resins. Our peptide synthesis platform applies high-efficiency coupling reagents and continuous monitoring to suppress deletion sequences across the 52-residue backbone, protecting the oxidation-sensitive Met5 residue throughout elongation.
Yes. Forming the native 6-residue disulfide ring between Cys16 and Cys21 requires precise regioselective oxidation. Our peptide modification services employ directed oxidative cyclization protocols in dilute solution to prevent intermolecular polymerization, verifying correct disulfide connectivity via peptide mapping and high-resolution LC-MS/MS.
Our manufacturing infrastructure scales production from milligram-level analytical batches to multigram and kilogram commercial quantities. We optimize liquid-phase handling and large-scale preparative HPLC purification, with validated protocols for counter-ion exchange (such as TFA removal to acetate), ensuring strict lot-to-lot consistency.
We operate as an integrated technical partner providing complete peptide CDMO solutions. Our team manages sequence optimization, folding verification, impurity profiling, analytical method validation, and regulatory documentation to advance preclinical and commercial peptide programs.
Adrenomedullin (1-52), human (CAS 148498-78-6) is a 52-residue regulatory peptide amide containing an essential intramolecular disulfide bridge between Cys16 and Cys21. Synpeptide provides comprehensive synthetic solutions for this target molecule. The dual challenges of assembling a 52-residue chain and forming an exact intramolecular macrocycle demonstrate our technical expertise in complex peptide manufacturing and CDMO services.
Constructing a 52-amino acid sequence requires precise control over coupling efficiency and steric hindrance to prevent on-resin aggregation. Our custom peptide synthesis platform utilizes optimized Solid-Phase Peptide Synthesis (SPPS) protocols on low-loading amide resins. By implementing high-efficiency coupling reagents, temperature control, and inert atmosphere handling to preserve the Met5 residue, we ensure high-fidelity assembly, consistently delivering raw materials with stringent purity specifications (typically ≥95% or ≥98% via HPLC).
The biological activity and structural integrity of Adrenomedullin (1-52) depend on its native Cys16-Cys21 disulfide bridge and C-terminal amide. Mispaired disulfide isomers and oligomeric aggregates represent significant analytical impurities. Through our peptide modification services, we utilize directed oxidative folding in high-dilution regimes. We verify disulfide connectivity and structural conformation using high-resolution LC-MS/MS, peptide mapping, and reduction-alkylation assays.
Transitioning a long, disulfide-constrained peptide from laboratory quantities to commercial production requires rigorous chemical engineering. Scaling up requires balancing folding kinetics against concentration-dependent multimerization. We execute large-scale peptide synthesis for Adrenomedullin (1-52) using high-capacity preparative HPLC purification and controlled lyophilization. Our infrastructure supports batch scaling from milligrams to kilograms, maintaining reproducible monomer yields and exact counter-ion specifications (including acetate conversion).
We provide full structural engineering and analytical documentation as an integrated peptide CDMO. Our development teams assist pharmaceutical partners with process optimization, stability testing, impurity identification, and analytical method validation. Every batch is released with comprehensive documentation—including COA, HPLC purity traces, and exact mass confirmation—ensuring regulatory alignment for downstream therapeutic programs.
