Teverelix

Teverelix, an efficacious biomedical medication extensively employed for managing hormone-dependent malignancies including prostate cancer, manifests its therapeutic effects by impeding the functioning of gonadotropin-releasing hormone (GnRH) receptors. Consequently, a decrease in testosterone synthesis and subsequent suppression of neoplastic expansion occur.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R2065

CAS No:151272-78-5

Chemical Name:(2S)-1-[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2R)-2-[[(2R)-2-acetamido-3-naphthalen-2-ylpropanoyl]amino]-3-(4-chlorophenyl)propanoyl]amino]-3-pyridin-3-ylpropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-6-(carbamoylamino)hexanoyl]amino]-4-methylpentanoyl]amino]-6-(propan-2-ylamino)hexanoyl]-N-[(2R)-1-amino-1-oxopropan-2-yl]pyrrolidine-2-carboxamide

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cGMP Peptide
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M.F/Formula
C74H100ClN15O14
M.W/Mr.
1459.13

Teverelix is a synthetic decapeptide belonging to the class of gonadotropin-releasing hormone (GnRH) antagonists, designed to modulate the activity of the hypothalamic-pituitary-gonadal axis. Characterized by its ability to bind competitively to GnRH receptors, Teverelix effectively inhibits endogenous GnRH action, thereby regulating downstream secretion of luteinizing hormone (LH) and follicle-stimulating hormone (FSH). Its chemical structure and receptor affinity render it a valuable tool for investigating peptide-receptor interactions, endocrine signaling pathways, and the physiological regulation of reproductive hormones. As a research-use-only compound, Teverelix is widely utilized in both fundamental and applied studies within endocrinology, peptide pharmacology, and molecular biology.

Receptor binding studies: As a potent GnRH antagonist, Teverelix is frequently employed in in vitro and ex vivo receptor binding assays to elucidate the dynamics of GnRH receptor interactions. Researchers use it to characterize ligand-receptor affinity, competitive inhibition profiles, and receptor occupancy, providing critical insights into receptor pharmacology and peptide ligand specificity. These studies support the development of new antagonists and inform the design of receptor-targeted biochemical assays.

Endocrine pathway modulation: Teverelix serves as an effective molecular tool for dissecting the regulatory mechanisms governing the hypothalamic-pituitary-gonadal axis. By selectively blocking GnRH receptor activation, it enables researchers to transiently suppress LH and FSH secretion in animal models or cell-based systems. This controlled inhibition allows for the investigation of downstream hormonal responses, feedback mechanisms, and the physiological consequences of disrupted GnRH signaling, contributing to a deeper understanding of endocrine homeostasis.

Peptide structure-activity relationship (SAR) analysis: Due to its well-defined sequence and functional activity, Teverelix is commonly included in structure-activity relationship studies focused on peptide therapeutics and receptor antagonists. By comparing its molecular features with those of related analogs, scientists can identify key amino acid residues responsible for receptor binding, antagonist potency, and metabolic stability. These SAR investigations drive the rational design of next-generation peptide antagonists with optimized properties.

Peptide synthesis validation: Laboratories involved in solid-phase peptide synthesis utilize Teverelix as a reference standard or benchmarking compound. Its established sequence and robust biological activity make it suitable for validating synthetic protocols, optimizing purification strategies, and calibrating analytical methods such as HPLC and mass spectrometry. Such applications are crucial for ensuring reproducibility and quality control in peptide production workflows.

Endocrine function research: In experimental models, Teverelix is used to transiently modulate reproductive hormone levels, enabling the study of physiological and molecular effects resulting from altered gonadotropin secretion. Researchers leverage its antagonistic properties to probe the roles of LH and FSH in reproductive tissue development, hormone-dependent gene expression, and feedback regulation. These investigations provide important mechanistic insights into reproductive biology and endocrine system function, supporting broader research in molecular endocrinology and hormone signaling.

InChI
InChI=1S/C74H100ClN15O14/c1-43(2)35-57(66(96)84-56(19-10-11-32-79-44(3)4)73(103)90-34-14-20-63(90)72(102)81-45(5)64(76)94)85-65(95)55(18-9-12-33-80-74(77)104)83-68(98)59(38-48-24-29-54(93)30-25-48)88-71(101)62(42-91)89-70(100)61(40-50-15-13-31-78-41-50)87-69(99)60(37-47-22-27-53(75)28-23-47)86-67(97)58(82-46(6)92)39-49-21-26-51-16-7-8-17-52(51)36-49/h7-8,13,15-17,21-31,36,41,43-45,55-63,79,91,93H,9-12,14,18-20,32-35,37-40,42H2,1-6H3,(H2,76,94)(H,81,102)(H,82,92)(H,83,98)(H,84,96)(H,85,95)(H,86,97)(H,87,99)(H,88,101)(H,89,100)(H3,77,80,104)/t45-,55-,56+,57+,58-,59+,60-,61-,62+,63+/m1/s1
InChI Key
NOENHWMKHNSHGX-IAOPALDYSA-N
Canonical SMILES
CC(C)CC(C(=O)NC(CCCCNC(C)C)C(=O)N1CCCC1C(=O)NC(C)C(=O)N)NC(=O)C(CCCCNC(=O)N)NC(=O)C(CC2=CC=C(C=C2)O)NC(=O)C(CO)NC(=O)C(CC3=CN=CC=C3)NC(=O)C(CC4=CC=C(C=C4)Cl)NC(=O)C(CC5=CC6=CC=CC=C6C=C5)NC(=O)C
Isomeric SMILES
C[C@H](C(=O)N)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCCNC(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CCCCNC(=O)N)NC(=O)[C@H](CC2=CC=C(C=C2)O)NC(=O)[C@H](CO)NC(=O)[C@@H](CC3=CN=CC=C3)NC(=O)[C@@H](CC4=CC=C(C=C4)Cl)NC(=O)[C@@H](CC5=CC6=CC=CC=C6C=C5)NC(=O)C

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