342878-90-4

Usage

Uses

Used in Pharmaceutical Industry:
UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT) is used as a therapeutic agent for its potential role in treating cardiovascular diseases, inflammation, and pain modulation. Its vasodilatory effects and involvement in physiological processes make it a promising candidate for the development of new drugs targeting these conditions.
Used in Research and Development:
UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT) is used as a research tool for studying the molecular mechanisms underlying its effects on cardiovascular function, smooth muscle contraction, inflammation, and pain modulation. This helps in understanding the pathophysiology of various diseases and identifying potential therapeutic targets.
Used in Drug Discovery:
UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT) is used as a target for drug discovery, as its involvement in the pathophysiology of various diseases suggests that modulating its activity or signaling pathways could lead to the development of novel therapeutic agents.
Used in Diagnostics:
UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT) can be used as a biomarker for the diagnosis and monitoring of diseases associated with its dysregulation, such as cardiovascular disorders, inflammation, and pain-related conditions.
Used in Toxicology Studies:
UROTENSIN II-RELATED PEPTIDE (HUMAN, MOUSE, RAT) can be used in toxicology studies to evaluate the safety and potential side effects of drugs targeting the urotensin II receptor or its signaling pathways, ensuring the development of safe and effective therapeutic agents.

Upstream product

• 68858-20-8 Fmoc-Val-OH 
• 35661-39-3 N-[(9H-fluoren-9-ylmethoxy)carbonyl]-L-alanine 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 103213-32-7 N-(9-fluorenylmethoxycarbonyl)-S-trityl-L-cysteine 
• 143824-78-6 3-[(S)-2-carboxy-2-(9H-fluoren-9-ylmethoxycarbonylamino)ethyl]indole-1-carboxylic acid tert-butyl ester 
• 575465-18-8 H-Ala-Cys-Phe-Trp-Lys-Tyr-Cys-Val-OH 
• 1421468-92-9 C₆₇H₈₄N₁₂O₁₂S₂ 

Relevant academic research and scientific papers

Functional Selectivity Revealed by N-Methylation Scanning of Human Urotensin II and Related Peptides

In accordance with their common but also divergent physiological actions, human urotensin II (1) and urotensin II-related peptide (2) could stabilize specific urotensin II receptor (UTR) conformations, thereby activating different signaling pathways, a feature referred to as biased agonism or functional selectivity. Sequential N-methylation of the amides in the conserved core sequence of 1, 2, and fragment U-II4-11 (3) shed light on structural requirements involved in their functional selectivity. Thus, 18 N-methylated UTR ligands were synthesized and their biological profiles evaluated using in vitro competition binding assays, ex vivo rat aortic ring bioassays and BRET-based biosensor experiments. Biological activity diverged from that of the parent structures contingent on the location of amide methylation, indicating relevant hydrogen-bond interactions for the function of the endogenous peptides. Conformational analysis of selected N-methyl analogs indicated the importance of specific amide residues of 2 for the distinct pharmacology relative to 1 and 3.

Agonists and antagonists of the urotensinergic system

Novel urotensin II receptor (UT) agonists and antagonists are described herein. More specifically, novel derivatives of urotensin II-related peptide (URP) are described herein.

An investigation into the origin of the biased agonism associated with the urotensin II receptor activation

The urotensin II receptor (UTR) has long been studied mainly for its involvement in the cardiovascular homeostasis both in health and disease state. Two endogenous ligands activate UTR, i.e. urotensin II (U-II) and urotensin II-related peptide (URP). Exte

Eco-friendly combination of the immobilized PGA enzyme and the s-phacm protecting group for the synthesis of cys-containing peptides

Enzyme-labile protecting groups have emerged as a green alternative to conventional protecting groups. These groups introduce a further orthogonal dimension and eco-friendliness into protection schemes for the synthesis of complex polyfunctional organic molecules. S-Phacm, a Cys-protecting group, can be easily removed by the action of a covalently immobilized PGA enzyme under very mild conditions. Herein, the versatility and reliability of an eco-friendly combination of the immobilized PGA enzyme and the S-Phacm protecting group has been evaluated for the synthesis of diverse Cys-containing peptides.