β-Casomorphin, human is an opioid peptide, acts as an agonist of opioid receptor.
CAT No: R1792
CAS No:102029-74-3
Synonyms/Alias:102029-74-3;H-Tyr-Pro-Phe-Val-Glu-Pro-Ile-OH;beta-Casomorphin, human;Casomorphin;2-[[1-[2-[[2-[[2-[[1-[2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-phenylpropanoyl]amino]-3-methylbutanoyl]amino]-4-carboxybutanoyl]pyrrolidine-2-carbonyl]amino]-3-methylpentanoic acid;DTXSID50403148;Tyrosylprolylphenylalanylvalyl-alpha-glutamylprolylisoleucine;(S)-4-((S)-2-((S)-2-((S)-1-((S)-2-Amino-3-(4-hydroxyphenyl)Propanoyl)pyrrolidine-2-carboxamido)-3-phenylPropanamido)-3-methylbutanamido)-5-((S)-2-(((1S,2S)-1-carboxy-2-methylbutyl)carbamoyl)pyrrolidin-1-yl)-5-oxopentanoic acid;b-Casomorphin, human;beta-Casomorphin human;??-Casomorphin, human;beta-Casomorphin (human);Human ??-casomorphin 7;Human beta casomorphin 7;b-Casomorphin, human(TFA);DTXCID70354002;CHEBI:172843;AKOS040759189;FC73316;2-{[1-(2-{2-[2-({1-[2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidin-2-yl}formamido)-3-phenylpropanamido]-3-methylbutanamido}-4-carboxybutanoyl)pyrrolidin-2-yl]formamido}-3-methylpentanoic acid;DA-59355;TS-09693;Human b-casomorphin 7Human b-casomorphin 7;
β-Casomorphin, human is a naturally occurring opioid peptide derived from the enzymatic digestion of human milk casein. As a member of the casomorphin family, this bioactive peptide is characterized by its unique amino acid sequence, which imparts specific affinity for opioid receptors. The compound has garnered significant research interest due to its physiological relevance in modulating neural, gastrointestinal, and immune functions. Its ability to interact with endogenous opioid systems makes it a valuable tool for investigating peptide-receptor interactions, neuromodulatory pathways, and the broader implications of dietary peptides in human biology.
Receptor binding studies: β-Casomorphin, human is widely utilized in receptor binding assays to elucidate the selectivity and affinity of opioid peptides for various receptor subtypes, including μ-, δ-, and κ-opioid receptors. By serving as a defined ligand, it enables researchers to map receptor distribution, determine binding kinetics, and assess the competitive interactions between endogenous and exogenous peptides. These investigations provide foundational insights into the molecular mechanisms governing opioid signaling and facilitate the development of novel modulators for research purposes.
Neuropharmacological research: The peptide's structural similarity to endogenous opioid ligands allows it to serve as a model compound in neuropharmacological studies. Researchers employ it to investigate the role of opioid peptides in modulating synaptic transmission, pain perception, and behavioral responses in vitro and in animal models. Its application extends to dissecting the influence of dietary-derived peptides on neurochemical pathways, offering a controlled system for exploring the physiological consequences of peptide absorption and central nervous system activity.
Gastrointestinal physiology: β-Casomorphin, human is instrumental in studies examining the impact of milk-derived peptides on gut function. Due to its resistance to rapid enzymatic degradation, it provides a model for assessing peptide transport across intestinal barriers, interaction with enteric opioid receptors, and modulation of gastrointestinal motility. Such research contributes to a deeper understanding of the relationship between dietary proteins, peptide bioavailability, and gut-brain communication.
Immunomodulation research: The interaction of opioid peptides with immune cells is an area of growing scientific interest. β-Casomorphin, human serves as a probe in immunological studies to evaluate its effects on cytokine release, lymphocyte activity, and the regulation of immune responses. By utilizing this peptide, investigators can delineate the pathways by which opioid receptor engagement influences immune cell signaling, thereby advancing knowledge of neuroimmune interactions.
Peptide metabolism and enzymology: As a substrate in enzymatic assays, β-Casomorphin, human provides a reliable system for characterizing the activity of peptidases and proteases involved in dietary protein processing. Its defined sequence and known cleavage sites make it suitable for kinetic studies, inhibitor screening, and the identification of novel enzymes. These applications support the broader field of peptide metabolism research, facilitating the discovery of factors that govern peptide stability, absorption, and bioactivity in biological systems.
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