Historphin offers a peptide motif with diverse functional groups that influence folding, solubility, and molecular recognition. Researchers investigate its conformational transitions and hydrogen-bond networks. Its amphipathic character aids binding-site modeling. Applications span structural biology, peptide engineering, and sequence-activity studies.
CAT No: R2342
CAS No:105250-85-9
Synonyms/Alias:105250-85-9;Historphin;Osteogenic Growth Peptide (10-14);Tyrosyl-glycyl-phenylalanyl-glycyl-glycine;Tyr-gly-phe-gly-gly;H-Tyr-Gly-Phe-Gly-Gly-OH;ogp(10-14);2-[[2-[[(2S)-2-[[2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]amino]-3-phenylpropanoyl]amino]acetyl]amino]acetic acid;Osteogenic Growth Peptide (10-14) trifluoroacetate salt;Glycine, N-(N-(N-(N-L-tyrosylglycyl)-L-phenylalanyl)glycyl)-;CHEMBL43978;DTXSID10909398;Osteogenic growth peptide(10-14);AKOS040755928;DA-76478;FO109638;MS-29276;H-Tyr-Gly-Phe-Gly-Gly-OH; H-YGFGG-OH;HY-107024;CS-0027162;G13481;N-[2-({2-[(2-{[2-Amino-1-hydroxy-3-(4-hydroxyphenyl)propylidene]amino}-1-hydroxyethylidene)amino]-1-hydroxy-3-phenylpropylidene}amino)-1-hydroxyethylidene]glycine;
Historphin, a synthetic peptide analog of the endogenous opioid peptide family, has garnered significant attention in biochemical and pharmacological research due to its unique structure and receptor-binding properties. As a member of the enkephalin-related peptide group, Historphin is characterized by its ability to interact with multiple opioid receptor subtypes, offering a valuable tool for dissecting the complex signaling pathways associated with pain modulation, stress response, and neurochemical communication. Its sequence and conformational flexibility enable researchers to explore receptor selectivity, ligand-receptor dynamics, and peptide stability, making it a versatile compound for in vitro and in vivo studies. The high affinity of Historphin for specific opioid receptors, coupled with its resistance to rapid enzymatic degradation, further enhances its utility in experimental settings where prolonged bioactivity is desirable.
Neuroscience research: In the field of neuroscience, Historphin serves as an important probe for elucidating the molecular mechanisms underlying opioid receptor-mediated signaling. By applying this peptide to cultured neuronal cells or brain tissue preparations, scientists can investigate the downstream effects of receptor activation, such as changes in intracellular calcium levels or modulation of neurotransmitter release. These studies contribute to a deeper understanding of how endogenous opioid peptides regulate synaptic transmission and neuronal excitability, offering insights into the physiological processes governing pain perception, mood regulation, and addiction pathways.
Pharmacology studies: Within pharmacological research, Historphin is frequently utilized to assess the potency and selectivity of novel opioid receptor ligands. Due to its well-defined structure and receptor interaction profile, it acts as a reference compound in competitive binding assays, enabling the comparison of new drug candidates' efficacy and affinity. Researchers can also employ Historphin in functional assays to monitor receptor activation, G-protein coupling, and downstream signaling events, facilitating the identification of compounds with desirable pharmacodynamic properties. Its application in these studies accelerates the drug discovery process and aids in the rational design of targeted therapeutics.
Peptide structure-activity relationship (SAR) analysis: The unique sequence of Historphin allows for detailed structure-activity relationship investigations, where systematic modifications to its amino acid composition can reveal critical determinants of receptor binding and biological activity. By synthesizing and testing analogs with specific substitutions, scientists can map the molecular features essential for high-affinity interaction with opioid receptors. These SAR studies not only advance the fundamental understanding of peptide-receptor recognition but also inform the development of optimized ligands with improved selectivity and stability.
Biochemical assay development: Historphin is a valuable standard in the development and validation of biochemical assays aimed at quantifying opioid receptor activity. Its consistent performance in receptor binding and signaling assays ensures reliable calibration and benchmarking of assay systems. Laboratories frequently incorporate this peptide into assay protocols to establish baseline responses, assess assay sensitivity, and verify reproducibility across experimental runs. The availability of Historphin as a reference material streamlines assay optimization and supports the generation of high-quality, reproducible data in opioid research.
Receptor localization and imaging: In addition to its functional applications, Historphin can be conjugated to fluorescent or radioactive labels for use in receptor localization and imaging studies. By tagging the peptide, researchers can visualize the distribution and density of opioid receptors in various tissues or cell types using microscopy or autoradiography techniques. Such imaging approaches provide spatial resolution of receptor expression patterns, contributing to the mapping of opioid signaling networks within the central nervous system and peripheral tissues. The ability to track the binding and internalization of labeled Historphin enhances the understanding of receptor trafficking and cellular responses to opioid peptides.
Overall, Historphin stands as a multifaceted tool for advancing opioid receptor research across multiple scientific disciplines. Its applications span from probing fundamental neurobiological mechanisms to supporting the development of innovative pharmacological agents and analytical methodologies. By facilitating the exploration of receptor signaling, ligand interactions, and peptide dynamics, Historphin continues to drive progress in both basic and applied research, ultimately broadening our knowledge of opioid system biology and its therapeutic potential.
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