L-Ala(10)-Cetrorelix introduces an alanine substitution at position ten within the cetrorelix framework. The change influences steric profile, local hydrophobicity, and conformational stability. Researchers compare its structural and chromatographic characteristics with native analogs. Applications include SAR analysis, impurity profiling, and analog development.
CAT No: Z10-101-175
Synonyms/Alias:Ac-D-2Nal-D-Phe(4-Cl)-D-3Pal-Ser-Tyr-D-Cit-Leu-Arg-Pro-Ala-NH2; (S)-N-((S)-1-amino-1-oxopropan-2-yl)-1-((2S,5S,8R,11S,14S,17R,20R,23R)-20-(4-chlorobenzyl)-2-(3-((diaminomethylene)amino)propyl)-11-(4-hydroxybenzyl)-14-(hydroxymethyl)-5-isobutyl-23-(naphthalen-2-ylmethyl)-4,7,10,13,16,19,22,25-octaoxo-17-(pyridin-3-ylmethyl)-8-(3-ureidopropyl)-3,6,9,12,15,18,21,24-octaazahexacosanoyl)pyrrolidine-2-carboxamide; N-acetyl-3-(2-naphthyl)-D-alanyl-4-chloro-D-phenylalanyl-3-(3-pyridyl)-D-alanyl-L-seryl-L-tyrosyl-D-citrullyl-L-leucyl-L-arginyl-L-prolyl-L-alaninamide
L-Ala(10)-Cetrorelix, also known as decapeptide cetrorelix with an L-alanine substitution at the tenth position, is a synthetic peptide analog widely employed in biochemical and pharmacological research. Its structure is based on modifications of natural gonadotropin-releasing hormone (GnRH) antagonists, which enables it to effectively inhibit the action of endogenous GnRH in various experimental settings. The substitution of L-alanine at the tenth position enhances its stability and bioactivity, making it a preferred tool for studies requiring precise modulation of peptide-receptor interactions. Researchers value L-Ala(10)-Cetrorelix for its high specificity, resistance to enzymatic degradation, and ability to maintain functional integrity under a range of laboratory conditions.
Reproductive Endocrinology Research: L-Ala(10)-Cetrorelix is frequently utilized in reproductive endocrinology studies due to its potent antagonistic effects on GnRH receptors. By blocking the GnRH receptor, it allows scientists to investigate the regulation of luteinizing hormone (LH) and follicle-stimulating hormone (FSH) secretion in vitro and in vivo. This application is crucial for dissecting the feedback mechanisms governing the hypothalamic-pituitary-gonadal axis, offering insights into hormone-dependent processes such as gametogenesis, steroidogenesis, and the timing of reproductive cycles. The use of this modified peptide provides a robust method for temporally controlling hormone release, facilitating the study of endocrine dynamics in animal models and cell cultures.
Cancer Biology Studies: Cetrorelix analogs, including L-Ala(10)-Cetrorelix, serve as valuable probes in cancer research, particularly in the context of hormone-dependent tumors. By inhibiting GnRH signaling, these peptides allow researchers to explore the role of gonadotropins in the growth and progression of certain cancers, such as those of the prostate, breast, and ovary. The ability to modulate hormonal environments in experimental systems enables the elucidation of molecular pathways involved in tumorigenesis, metastasis, and hormone-resistance mechanisms. Furthermore, this decapeptide is instrumental in developing new strategies for targeting hormone-responsive cancer cells, thereby advancing preclinical research and therapeutic innovation.
Signal Transduction Pathway Analysis: The unique properties of L-Ala(10)-Cetrorelix make it an effective tool for dissecting signal transduction pathways associated with GnRH receptor activation. By selectively blocking receptor-ligand interactions, it helps delineate downstream signaling events, such as the activation of G-proteins, second messenger cascades, and transcriptional responses. This application is particularly valuable for mapping the molecular networks that regulate cell proliferation, differentiation, and apoptosis in various tissue types. Researchers can employ the peptide to test hypotheses regarding receptor cross-talk, desensitization, and the integration of hormonal signals with other cellular stimuli, thus enhancing the understanding of complex regulatory systems.
Peptide-Receptor Interaction Studies: The modified structure of L-Ala(10)-Cetrorelix provides a model system for investigating the structural determinants of peptide-receptor binding. Scientists use it to perform binding assays, competition experiments, and structure-activity relationship analyses, which are essential for rational drug design and the development of next-generation GnRH antagonists. These studies contribute to the refinement of peptide therapeutics by identifying key residues responsible for receptor affinity, selectivity, and functional antagonism. The insights gained from such research have broad implications for the design of peptide-based modulators targeting other G-protein-coupled receptors.
Drug Screening and Development: L-Ala(10)-Cetrorelix is also incorporated into high-throughput screening platforms and preclinical evaluation protocols for novel compounds targeting GnRH pathways. Its well-characterized antagonistic profile allows it to serve as a reference compound or control in comparative assays, facilitating the identification of new molecules with improved potency, selectivity, or pharmacokinetic properties. By providing a reliable benchmark, it accelerates the discovery process and supports the optimization of candidate drugs for further investigation in diverse research domains, including reproductive health, oncology, and neuroendocrinology. The versatility and reliability of this peptide analog underscore its enduring value in scientific exploration and innovation.
2. Cationic cell-penetrating peptides are potent furin inhibitors
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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