D-Ser-Cetrorelix introduces a D-serine substitution that shifts stereochemistry and impacts hydrogen-bonding potential. Researchers use it to evaluate the role of chirality in receptor recognition and peptide folding. Applications include analog comparison, stability evaluation, and structural mapping.
CAT No: Z10-101-185
Synonyms/Alias:Ac-D-2Nal-D-Phe(4-Cl)-D-3Pal-D-Ser-Tyr-D-Cit-Leu-Arg-Pro-D-Ala-NH2;(S)-1-(((R)-2-((S)-2-((R)-2-((R)-2-((R)-2-((R)-2-acetamido-3-(naphthalen-2-yl)propanamido)-3-(4-chlorophenyl)propanamido)-3-(pyridin-3-yl)propanamido)-3-hydroxypropanamido)-3-(4-hydroxyphenyl)propanamido)-5-ureidopentanoyl)-L-leucyl-L-arginyl)-N-((R)-1-amino-1-oxopropan-2-yl)pyrrolidine-2-carboxamide;Cetrorelix D-Ser Isomeric Impurity
D-Ser-Cetrorelix is a synthetic peptide analog designed to modulate the activity of gonadotropin-releasing hormone (GnRH) receptors. Structurally, it incorporates a D-serine residue, which enhances its stability and receptor selectivity compared to native peptide sequences. As a decapeptide antagonist of GnRH, D-Ser-Cetrorelix plays a significant role in the study of reproductive endocrinology and neuroendocrine signaling. Its molecular configuration and resistance to enzymatic degradation make it a valuable tool for research applications requiring precise modulation of peptide hormone pathways.
Reproductive axis modulation: D-Ser-Cetrorelix is widely utilized in studies investigating the regulation of the hypothalamic-pituitary-gonadal (HPG) axis. By competitively inhibiting GnRH receptors, the peptide enables researchers to suppress downstream secretion of luteinizing hormone (LH) and follicle-stimulating hormone (FSH). This property is particularly useful for dissecting the mechanisms underlying gonadotropin release, feedback regulation, and the hormonal control of reproductive physiology in animal models and in vitro systems.
Peptide receptor pharmacology: The compound serves as a reference antagonist in receptor binding assays and functional studies aimed at characterizing GnRH receptor subtypes. Its high affinity and selectivity allow for detailed analysis of receptor-ligand interactions, desensitization kinetics, and signal transduction pathways. Researchers employ D-Ser-Cetrorelix to benchmark the efficacy of novel GnRH analogs, enabling comparative studies that inform the design of next-generation peptide therapeutics and research probes.
Peptide synthesis and analog development: Owing to its modified structure, D-Ser-Cetrorelix is frequently used as a template or standard in the synthesis of custom peptide analogs. Synthetic chemists leverage its sequence to explore the impact of specific amino acid substitutions, D-amino acid incorporation, and backbone modifications on biological activity and metabolic stability. These structure-activity relationship (SAR) investigations are essential for advancing peptide engineering and optimizing pharmacological profiles.
Endocrine signaling pathway analysis: The ability of D-Ser-Cetrorelix to selectively block GnRH-mediated signaling makes it a powerful tool for mapping downstream molecular events in endocrine tissues. By modulating receptor activation in controlled experimental settings, researchers can unravel the intricate cascade of intracellular messengers, gene expression changes, and feedback mechanisms that govern hormonal homeostasis. Such studies provide critical insights into the dynamics of neuropeptide signaling networks.
Cellular assay development: Laboratories involved in high-throughput screening and assay development utilize D-Ser-Cetrorelix as a control or calibrator in cellular systems expressing GnRH receptors. Its well-characterized inhibitory profile supports the validation of assay sensitivity, specificity, and reproducibility. The compound's stability and defined activity make it an ideal reference standard for optimizing protocols in receptor antagonist screening and functional genomics platforms.
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