Beta-Endorphin is a long, amphipathic peptide composed of hydrophobic, charged, and aromatic residues that support complex folding. Its extended sequence makes it valuable for studies of binding equilibria, conformational transitions, and multivalent interactions. Researchers analyze its hydrogen-bond networks and domain flexibility. Applications include structural biochemistry, peptide engineering, and sequence-function research.
CAT No: R2685
CAS No:60617-12-1
Synonyms/Alias:61214-51-5;beta-ENDORPHIN;BETA-ENDORPHIN HUMAN SYNTHETIC;beta-end;beta-Endorphin (sheep), 27-L-tyrosine-31-L-glutamic acid-;EINECS 262-330-3;60617-12-1;beta-Endorphin (human) trifluoroacetate salt;.beta.-endorphin;Endorphin, beta;UNII-3S51P4W3XQ;|A-Endorphin, human;??-Endorphin, human;?-ENDORPHIN;3S51P4W3XQ;GTPL1643;SCHEMBL6238339;CHEMBL1866903;27-L-Tyrosine-31-L-glutamic acid-beta-endorphin (sheep);beta-Endorphin (Human Synthetic);DTXSID30210135;DTXSID801053886;MFCD00076383;AKOS040740635;beta-Endorphin human, >=95% (HPLC);NCGC00163196-01;NCGC00163196-02;AS-83086;DA-68912;FE108749;F82167;262-330-3;
Beta-Endorphin is a naturally occurring endogenous opioid peptide, derived from the precursor protein proopiomelanocortin (POMC) and primarily produced in the pituitary gland and central nervous system. As a member of the endorphin family, it is recognized for its potent neuromodulatory and neuroregulatory properties, playing a critical role in pain modulation, stress response, and behavioral regulation. Its sequence and structure have made it a subject of significant interest in neurobiology, peptide signaling research, and studies exploring the molecular basis of opioid receptor interactions. Owing to its physiological relevance and unique biochemical characteristics, Beta-Endorphin is widely utilized in experimental settings seeking to unravel peptide-mediated processes and opioid signaling pathways.
Neuroscience research: Beta-Endorphin serves as a pivotal tool in elucidating the mechanisms of endogenous opioid signaling within the central nervous system. Researchers employ it in in vitro and in vivo studies to investigate synaptic transmission, neuronal excitability, and the modulation of neurotransmitter release. Its interactions with mu- and delta-opioid receptors allow for detailed analysis of pain perception, reward pathways, and the neurobiological underpinnings of mood and stress adaptation, providing a foundation for understanding complex neurophysiological phenomena.
Receptor binding assays: The peptide is frequently utilized in radioligand binding studies and receptor activation assays to characterize the affinity, selectivity, and efficacy of opioid receptors. By serving as a reference ligand or functional agonist, Beta-Endorphin enables the quantification of receptor-ligand interactions, supports the screening of novel opioid analogs, and facilitates structure-activity relationship (SAR) investigations. Its use in these assays is instrumental in mapping receptor pharmacology and advancing the development of receptor-targeted probes.
Peptide structure-function analysis: Beta-Endorphin is an exemplary model for probing the relationship between peptide sequence, conformation, and biological activity. Researchers leverage synthetic or recombinant forms of the peptide to study folding dynamics, post-translational modifications, and the impact of sequence alterations on receptor binding and activation. Such investigations contribute to a deeper understanding of peptide engineering principles and inform the rational design of bioactive peptide analogs with tailored pharmacological profiles.
Behavioral pharmacology: Experimental paradigms in behavioral neuroscience often incorporate Beta-Endorphin to assess its influence on learning, memory, stress responses, and motivational states in animal models. By administering the peptide and monitoring behavioral outcomes, scientists can dissect the roles of endogenous opioids in modulating affective and cognitive processes. These studies are essential for delineating the molecular substrates of behavior and for modeling neuropsychiatric conditions in preclinical research.
Analytical method development: The peptide is also employed as a standard or reference compound in the development and validation of bioanalytical methods, such as immunoassays, liquid chromatography, and mass spectrometry techniques. Its well-characterized properties and biological relevance make it suitable for calibrating detection systems, optimizing assay sensitivity, and ensuring specificity in the quantification of endogenous or exogenous opioid peptides in complex biological samples. This application supports advancements in biomarker discovery, pharmacokinetic studies, and peptide quantification in diverse research contexts.
3. Myotropic activity of allatostatins in tenebrionid beetles
4. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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