Gluten exorphin C is an opioid peptide derived from wheat gluten. Its IC50 values are 40 μM and 13.5 μM for μ opioid and δ opioid activities in the GPI and MVD assays, respectively.
CAT No: R1388
CAS No:142479-62-7
Synonyms/Alias:Gluten Exorphin C;142479-62-7;(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-1-[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoic acid;H-Tyr-Pro-Ile-Ser-Leu-OH;MFCD00237077;Tyr-Pro-Ile-Ser-Leu;CHEBI:168116;HY-P1596;AKOS040764111;DA-63807;FG108441;MS-30530;CS-0045223;G12529;Gluten Exorphin C (H-L-Tyr-L-Pro-L-Ile-L-Ser-L-Leu-OH);(2S)-2-[(2S)-2-[(2S,3S)-2-{[(2S)-1-[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]pyrrolidin-2-yl]formamido}-3-methylpentanamido]-3-hydroxypropanamido]-4-methylpentanoic acid;
Gluten Exorphin C is a bioactive peptide derived from the enzymatic digestion of gluten proteins, notably within the prolamin fraction of wheat. As an opioid peptide, it features a unique amino acid sequence that enables interaction with opioid receptors, imparting distinct physiological and biochemical activities. The compound has garnered significant interest in peptide biochemistry due to its role in modulating neurochemical pathways and its relevance to studies of food-derived bioactive molecules. Researchers utilize Gluten Exorphin C to explore the broader implications of dietary peptides on cellular signaling, neurotransmission, and metabolic regulation, making it a valuable tool in both fundamental and applied peptide research.
Peptide receptor interaction studies: Gluten Exorphin C serves as a model compound for investigating the binding affinity and selectivity of food-derived peptides toward opioid receptors. Its well-characterized sequence allows researchers to delineate the molecular determinants of receptor recognition, providing insight into the structure-activity relationships that govern peptide-receptor interactions. By employing this peptide in receptor binding assays, scientists can elucidate the mechanisms by which exogenous peptides influence endogenous opioid pathways, thereby advancing our understanding of neuropeptide signaling and its physiological consequences.
Neurochemical modulation research: The opioid-like activity of Gluten Exorphin C makes it a critical reagent for examining the effects of dietary peptides on neurotransmitter systems. In vitro and ex vivo studies frequently utilize this peptide to assess its impact on neuronal cells, synaptic transmission, and second messenger cascades. Such investigations help clarify how food-derived peptides may alter neurochemical homeostasis, offering valuable data for the broader field of nutritional neuroscience and peptide pharmacology.
Enzymatic digestion and bioavailability analysis: Gluten Exorphin C is widely used as a reference substrate in studies focused on gastrointestinal enzymatic processing of dietary proteins. By monitoring the generation and stability of this peptide during simulated digestion, researchers can evaluate the efficiency of proteolytic enzymes and the resulting bioactive peptide profiles. These experiments are essential for understanding the fate of food-derived peptides in the human digestive tract and for developing improved models of peptide absorption and metabolism.
Analytical method development: The unique sequence and bioactivity of Gluten Exorphin C make it an ideal standard for the development and validation of analytical techniques, such as high-performance liquid chromatography (HPLC) and mass spectrometry. Method optimization using this peptide enables precise quantification and detection of similar exorphins in complex biological or food matrices. Its use as a calibration standard supports advancements in peptide analytics, facilitating quality control and biomarker discovery efforts within food science and biochemical research.
Peptide synthesis and modification studies: Gluten Exorphin C is frequently employed in peptide synthesis research, where it serves as a benchmark for evaluating synthetic strategies, purification protocols, and structural modifications. Researchers utilize this peptide to test novel coupling reagents, assess post-synthetic modifications, and explore the effects of sequence alterations on bioactivity. Its role in synthesis-oriented studies contributes to the refinement of solid-phase peptide synthesis methodologies and the generation of new peptide analogs for functional investigation.
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