Teriparatide Impurity 3 (Teri-Met18(O)) features oxidation of methionine at position 18 to methionine sulfoxide. The modification increases polarity and perturbs local side-chain packing. Researchers monitor its formation to evaluate oxidative stability and degradation pathways. Applications include stress-testing studies, impurity specification, and redox-chemistry characterization in peptide formulations.
CAT No: Z10-101-228
Synonyms/Alias:Teriparatide Impurity 3 (Teri-Met 18(O)); L-seryl-L-valyl-L-seryl-L-glutamyl-L-isoleucyl-L-glutaminyl-L-leucyl-L-methionyl-L-histidyl-L-asparagyl-L-leucyl-glycyl-L-lysyl-L-histidyl-L-leucyl-L-asparagyl-L-seryl-L-methionyl(O)-L-glutamyl-L-arginyl-L-valyl-L-alpha-glutamyl-L-tryptophyl-L-leucyl-L-arginyl-L-lysyl-L-lysyl-L-leucyl-L-glutaminyl-L-alpha-aspartyl-L-valyl-L-histidyl-L-asparagyl-L-phenylalanine; Met(O)18-Teriparatide; H-Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-His-Leu-Asn-Ser-Met(O)-Glu-Arg-Val-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe-OH
Teriparatide Impurity 3 (Teri-Met 18(O)) is a synthetic peptide variant derived from the well-characterized sequence of teriparatide, a recombinant form of parathyroid hormone (PTH 1-34). As an impurity standard, this compound features a specific methionine oxidation at position 18, offering a structurally defined model for studying peptide oxidation and its impact on biological activity, structural integrity, and analytical detection. The precise modification present in Teri-Met 18(O) makes it a valuable reference material for peptide scientists aiming to understand degradation pathways, validate analytical methods, and ensure the quality of peptide-based therapeutics and research reagents.
Peptide impurity profiling: In peptide manufacturing and quality control, the presence and characterization of sequence-related impurities are critical for product safety and efficacy. Teri-Met 18(O) serves as a reference standard for the identification and quantification of oxidized methionine species in teriparatide preparations. Its use enables analytical chemists to calibrate and validate high-performance liquid chromatography (HPLC) and mass spectrometry (MS) methods, ensuring accurate detection and control of oxidative modifications during peptide synthesis and storage.
Analytical method development: The oxidized methionine residue within this impurity provides a relevant model for developing and optimizing analytical protocols targeting post-translational modifications in peptides. Researchers can employ Teri-Met 18(O) to assess method sensitivity, specificity, and robustness when distinguishing between native and oxidized forms of teriparatide or related peptides. This supports the advancement of reliable quality assessment tools essential for both research and industrial peptide production.
Peptide stability studies: Oxidative degradation is a common challenge in peptide formulation and storage. The availability of Teri-Met 18(O) allows formulation scientists to investigate the susceptibility of methionine residues to oxidation under various environmental conditions. By including this impurity in forced degradation studies, researchers can better understand the kinetics and mechanisms of peptide oxidation, informing the design of more stable peptide therapeutics and storage protocols.
Structure-activity relationship research: Modifications such as methionine oxidation can significantly alter the biological and physicochemical properties of peptides. Teri-Met 18(O) can be utilized in structure-activity relationship (SAR) studies to elucidate the impact of specific oxidative changes on receptor binding, conformational stability, and functional activity. Insights gained from such investigations contribute to the rational design of peptide analogs with improved performance and reduced susceptibility to degradation.
Peptide synthesis process validation: The use of well-characterized impurities like Teri-Met 18(O) is essential for validating peptide synthesis and purification processes. By intentionally spiking this impurity into production samples, process chemists can evaluate the efficiency of purification steps in removing oxidized byproducts. This information is vital for optimizing manufacturing protocols and ensuring batch-to-batch consistency in peptide product quality, ultimately supporting regulatory compliance and industry best practices.
3. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
4. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More