Orexin A (17-33), truncated form of orexin A, acts as potent and selective peptide orexin OX1 receptor antagonist.
OXA (17-33) is a synthetic peptide fragment corresponding to amino acid residues 17 through 33 of the orexin A neuropeptide. As a truncated analog of the endogenous orexin A, it retains portions of the biologically active sequence while lacking the full-length structure, making it a valuable tool for dissecting the structure-activity relationships of orexin signaling. The peptide is of particular interest in neurobiology and receptor pharmacology due to its selective interaction with orexin receptors and its utility in studying peptide-receptor binding dynamics. Researchers leverage OXA (17-33) to better understand the functional domains of orexin peptides, facilitating insights into neuropeptide signaling mechanisms and receptor specificity.
Receptor binding studies: OXA (17-33) serves as a specialized probe for investigating the binding affinity and selectivity of orexin receptors, particularly OX1R and OX2R. By comparing the biological activity of this truncated peptide to that of full-length orexin A, scientists can delineate essential regions required for receptor activation and binding. This approach aids in mapping the minimal active core of the peptide and elucidating the contribution of specific residues to ligand-receptor interactions, which is critical for the rational design of receptor modulators.
Structure-activity relationship analysis: The use of this peptide fragment enables systematic evaluation of how sequential truncations or modifications affect orexin A's biological functions. Through biochemical assays and cellular models, researchers can assess the impact of the 17-33 fragment on downstream signaling pathways. Such studies provide detailed information about the structural determinants of peptide activity, supporting the development of targeted analogs with desired pharmacological properties for experimental applications.
Peptide-receptor interaction modeling: OXA (17-33) is frequently employed in computational and experimental models to simulate and analyze peptide-receptor interactions at the molecular level. Its defined sequence allows for precise docking studies, mutagenesis experiments, and conformational analyses, which contribute to a deeper understanding of the molecular basis for receptor selectivity and activation. These findings are instrumental in advancing the field of neuropeptide pharmacology and in guiding the development of novel ligands.
Neuropeptide signaling research: As a representative fragment of orexin A, this peptide is utilized in research aimed at decoding the physiological and biochemical roles of orexin signaling in neuronal systems. By applying the 17-33 sequence in in vitro and ex vivo models, investigators can parse the contribution of specific peptide domains to overall neuropeptide function, receptor desensitization, and signaling cascade initiation. Such studies are essential for unraveling the complexity of neuropeptide-mediated communication in the central nervous system.
Peptide synthesis validation: OXA (17-33) is also used as a reference standard or intermediate in peptide synthesis laboratories. Its well-characterized sequence makes it suitable for optimizing solid-phase peptide synthesis protocols and validating analytical techniques such as mass spectrometry and high-performance liquid chromatography. By serving as a benchmark for synthetic fidelity and purity assessment, it supports the development and quality control of peptide-based research reagents.
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