Dermorphin, 4-Hyp(6)- is a dermorphin analogue containing 4-hydroxyproline at position 6, altering backbone rigidity and hydrogen-bonding characteristics. The modification influences β-turn formation and aromatic-hydrophobic packing. Researchers examine its structural distribution and receptor-binding determinants. Applications include opioid-peptide motif studies, structural refinement, and analog development.
CAT No: R2386
CAS No:77614-17-6
Synonyms/Alias:Dermorphin, 4-hyp(6)-;6-(4-Hyp)-dermorphin;77614-17-6;Dermorphin, 4-hydroxyproline(6)-;Dermorphin, 6-(trans-4-hydroxy-L-proline)-;DTXSID00228282;H-Tyr-D-Ala-Phe-Gly-Tyr-Hyp-Ser-NH2;DTXCID20150773;Tyr-D-Ala-Phe-Gly-Tyr-Hyp-Ser-NH2;
Dermorphin, 4-hyp(6) is a synthetic peptide analog derived from the naturally occurring opioid peptide dermorphin, featuring a hydroxyproline substitution at the sixth position. As a member of the opioid peptide family, this compound exhibits a unique structural profile that influences its interaction with opioid receptors, making it a valuable molecular tool in neuropharmacology and receptor biology. Its sequence modification, specifically the incorporation of 4-hydroxyproline, enables researchers to probe the structure-activity relationships of peptide ligands and to explore the functional consequences of amino acid substitutions within bioactive peptides. Owing to its well-defined peptide backbone and receptor selectivity, Dermorphin, 4-hyp(6) is utilized in a variety of biochemical and pharmacological research applications focused on opioid signaling and peptide-receptor interactions.
Receptor Binding Studies: Dermorphin analogs such as 4-hyp(6) are widely used in receptor binding assays to elucidate the molecular determinants of opioid receptor affinity and selectivity. The hydroxyproline substitution offers a means to systematically investigate how specific side-chain modifications alter ligand-receptor interactions, providing critical insights into the binding pocket architecture of mu-opioid receptors. These studies facilitate the mapping of key contact points and support the rational design of novel peptide ligands with tailored pharmacological profiles.
Peptide Structure-Activity Relationship (SAR) Research: The introduction of 4-hydroxyproline into the dermorphin sequence allows for detailed SAR analyses, enabling researchers to dissect the contributions of individual residues to overall bioactivity. By comparing the biological activity of this analog with that of the parent peptide and other derivatives, scientists can better understand the role of conformational rigidity, hydrogen bonding, and side-chain orientation in modulating receptor activation. Such investigations are instrumental in advancing peptide engineering and optimizing peptide-based tools for neurobiological research.
Opioid Signaling Pathway Exploration: In cellular and biochemical assays, this modified peptide serves as a probe to study downstream signaling events following opioid receptor engagement. Its unique structural features permit the assessment of G protein-coupled receptor (GPCR) activation, signal transduction specificity, and the modulation of intracellular effectors such as cyclic AMP, protein kinases, and ion channels. These experiments contribute to a deeper understanding of the molecular mechanisms underlying opioid-induced cellular responses and can reveal novel aspects of receptor function.
Peptide Stability and Metabolic Profiling: The incorporation of hydroxyproline into the peptide backbone offers a model system for evaluating the impact of non-canonical amino acids on peptide stability, proteolytic resistance, and metabolic fate. Researchers utilize this analog to assess degradation kinetics in various biological matrices, informing the development of more robust peptide probes and contributing to the broader field of peptide drug design. Such studies are essential for identifying sequence modifications that enhance peptide durability without compromising receptor affinity.
Tool Compound for Synthetic Peptide Libraries: Dermorphin, 4-hyp(6) is also employed as a reference compound or structural motif in the synthesis of peptide libraries aimed at discovering new bioactive sequences. Its defined modification serves as a benchmark for evaluating the effects of hydroxylated residues on peptide conformation, receptor interaction, and functional activity. This application supports high-throughput screening efforts in neurobiology, pharmacology, and peptide chemistry, driving the identification of innovative ligands with potential research utility.
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