Selective and potent antagonist of corticotropin-releasing factor receptor 2 (CRF2) (IC50 values are 1.3 and > 500 nM for CRF2 and CRF1 respectively) that antagonizes CRF2-mediated inhibition of gastric emptying.
CAT No: R1100
CAS No:681260-70-8
Synonyms/Alias:astressin-2B;ASTRESSIN 2B;681260-70-8;cyclo(31-34)(Phe11,His12,CMeLeu13,39,Nle17,Glu31,Lys34) Ac-sauvagine(8-40);Cyclo(31-34)(Phe(11),His(12),CMeLeu(13,39),Nle(17),Glu(31),Lys(34)) Ac-sauvagine (8-40);MFCD05665271;DA-61276;Cyclo(31-34)[D-Phe11,His12,C(alpha)MeLeu13,39,Nle17,Glu31,Lys34]Ac-Svg(8-40) trifluoroacetate salt;
Astressin 2B is a synthetic peptide antagonist specifically designed to target the corticotropin-releasing factor receptor type 2 (CRF2). As a member of the CRF family of peptide modulators, it exhibits high selectivity for CRF2 over CRF1, making it a valuable research tool for dissecting the physiological and biochemical roles of CRF2-mediated signaling. Its structural features and receptor specificity have positioned it as a key molecule for investigating stress response pathways, neuroendocrine regulation, and related cellular processes in both in vitro and in vivo experimental models. The ability to modulate CRF2 activity with precision has expanded the scope of research into stress adaptation, metabolic regulation, and neuropeptide receptor pharmacology.
Receptor Pharmacology: Astressin 2B is widely utilized in receptor pharmacology studies to elucidate the binding characteristics, signaling mechanisms, and downstream effects of CRF2 activation or inhibition. By serving as a selective antagonist, it enables researchers to differentiate CRF2-mediated responses from those mediated by CRF1, facilitating the mapping of receptor-specific pathways in various cell types and tissue systems. This selectivity is critical for understanding the nuanced roles of CRF2 in neuroendocrine circuits and for validating receptor subtype contributions in complex physiological contexts.
Stress Response Research: In the context of stress biology, this peptide is instrumental for probing the involvement of CRF2 in the regulation of hypothalamic-pituitary-adrenal (HPA) axis activity and stress-related neuroendocrine responses. By blocking CRF2, scientists can assess the receptor's influence on hormone secretion, neuronal activation, and adaptive responses to acute or chronic stressors. Such studies provide valuable insights into the distinct contributions of CRF receptor subtypes in stress adaptation and resilience, supporting the development of new hypotheses regarding stress-related disorders.
Metabolic Regulation Studies: Astressin 2B has proven to be a useful probe in metabolic research, particularly in investigations of appetite control, energy balance, and glucose homeostasis. Its ability to inhibit CRF2 signaling allows researchers to examine how this pathway modulates feeding behavior, insulin sensitivity, and metabolic adaptation under various physiological and pathophysiological conditions. These findings contribute to a deeper understanding of neuropeptide regulation in metabolic syndrome, obesity, and related metabolic disturbances.
Behavioral Neuroscience: The peptide's selectivity for CRF2 makes it valuable for behavioral neuroscience studies aimed at dissecting the molecular substrates of anxiety, mood regulation, and emotional processing. By selectively antagonizing CRF2, it is possible to determine the receptor's role in modulating behavioral responses to environmental challenges, social interactions, and emotional stimuli. Such research is essential for clarifying the neurobiological foundations of affective behaviors and for identifying potential molecular targets for future investigation.
Peptide Mechanism Exploration: As a synthetic peptide tool, Astressin 2B is also employed in studies aimed at understanding structure-activity relationships within the CRF peptide family. Its use in peptide mapping, receptor binding assays, and conformational analyses provides critical insights into the determinants of receptor selectivity, affinity, and functional antagonism. These mechanistic explorations support the rational design of next-generation peptide modulators and advance the broader field of peptide-receptor interaction research.
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