An impurity of Felypressin. Felypressin is a Vasopressin 1 agonist, and will thus have effects at all Arginine vasopressin receptor 1As. It physiologically effects on vascular SMC's due to the form in which it is administered. Its receptors are found in various sites around the body. The major points include the CNS, Liver, Anterior Pituitary, Muscle (both vascular and non-vascular smooth muscle), and Platelets (CLAMP).
CAT No: 10-101-191
Felypressin Impurity D is a synthetic peptide derivative structurally related to the vasopressin analog felypressin. As an identified process impurity, it arises during the chemical synthesis or degradation of felypressin, a peptide widely utilized in research on vasoconstrictive mechanisms and as a model for peptide hormone analogs. The presence and characterization of such impurities are critical for ensuring the reliability and interpretability of peptide-based studies, as minor sequence variations can significantly alter biological activity, receptor affinity, or stability. Felypressin Impurity D, therefore, holds particular value in analytical method development, quality control, and mechanistic investigations within peptide research and pharmaceutical development environments.
Analytical method validation: Felypressin Impurity D serves as a crucial reference standard in the validation and optimization of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its inclusion enables precise identification, quantification, and separation of structurally similar peptide impurities from the main active compound. By providing a well-characterized impurity profile, researchers can assess the specificity, sensitivity, and robustness of their analytical protocols, thereby ensuring the integrity of peptide quality control processes.
Peptide synthesis optimization: The availability of this impurity facilitates detailed studies into the synthetic pathways and degradation routes of felypressin and related peptides. By monitoring the formation of Felypressin Impurity D during various stages of solid-phase or solution-phase peptide synthesis, chemists can identify process inefficiencies, side reactions, or conditions that favor impurity generation. Such insights are instrumental in refining synthetic strategies, improving overall yield and purity, and minimizing unwanted byproducts in laboratory and industrial peptide production.
Impurity profiling and regulatory research: In the context of pharmaceutical development, comprehensive impurity profiling is a fundamental aspect of product characterization and safety assessment. Felypressin Impurity D enables the establishment of impurity thresholds, supports forced degradation studies, and aids in the development of impurity control strategies. By systematically studying its behavior under different storage or stress conditions, researchers can anticipate potential stability concerns and inform the design of robust peptide formulations.
Structure-activity relationship studies: The presence of specific sequence or structural modifications in Felypressin Impurity D allows for targeted structure-activity relationship (SAR) investigations. By comparing the biological or physicochemical properties of this impurity with those of the parent peptide, researchers can elucidate the impact of subtle changes on receptor binding, functional activity, or metabolic stability. Such studies contribute to a deeper understanding of peptide-receptor interactions and guide the rational design of novel analogs with optimized profiles.
Reference material for peptide research: Felypressin Impurity D is also valuable as a reference compound in broader peptide research applications. Its well-defined structure and origin make it suitable for benchmarking analytical performance, calibrating detection systems, or serving as a control in experimental protocols involving vasopressin analogs. The use of authentic impurities in research settings enhances data reliability and supports rigorous scientific evaluation of peptide-based materials.
3. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
4. The spatiotemporal control of signalling and trafficking of the GLP-1R
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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