[Des-octanoyl]-Ghrelin (rat) is a non-acylated, major circulating isoform of ghrelin that does not bind to the ghrelin receptor (GHS-R1a), nor induce growth hormone release.
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CAT No: 10-101-320
CAS No:307950-60-3
Synonyms/Alias:307950-60-3;GLY-SER-SER-PHE-LEU-SER-PRO-GLU-HIS-GLN-LYS-ALA-GLN-GLN-ARG-LYS-GLU-SER-LYS-LYS-PRO-PRO-ALA-LYS-LEU-GLN-PRO-ARG;AKOS024457353;Alternative Name: Des-acyl ghrelin (rat);FD109777;[Des-octanoyl] -Ghrelin pound rat pound(c) TFA;(Des-octanoyl)-Ghrelin (mouse, rat) trifluoroacetate salt;H-Gly-Ser-Ser-Phe-Leu-Ser-Pro-Glu-His-Gln-Lys-Ala-Gln-Gln-Arg-Lys-Glu-Ser- Lys-Lys-Pro-Pro-Ala-Lys-Leu-Gln-Pro-Arg-OH; H-GSSFLSPEHQK AQQRKESKKPPAKLQPR-OH;
[Des-octanoyl]-Ghrelin (rat) is a synthetic peptide analog derived from the endogenous hormone ghrelin, with the octanoyl modification specifically removed from its structure. As a non-acylated form of ghrelin, it retains the core peptide backbone but lacks the essential fatty acid modification required for activating the canonical ghrelin receptor (GHS-R1a). This structural distinction makes [Des-octanoyl]-Ghrelin particularly valuable for dissecting the biological roles of acylated versus non-acylated ghrelin isoforms in rodent models. Its unique properties have positioned it as a crucial tool in peptide research, especially for elucidating the non-endocrine functions, receptor interactions, and signaling pathways associated with ghrelin and its derivatives.
Receptor binding studies: [Des-octanoyl]-Ghrelin is widely employed in receptor binding assays to differentiate between acylated and non-acylated ghrelin interactions with the growth hormone secretagogue receptor (GHS-R1a) and related targets. By comparing the binding affinities and downstream signaling responses of this peptide with its acylated counterpart, researchers can clarify the structural requirements for receptor activation and identify potential alternative binding partners. Such studies are instrumental in mapping the molecular determinants of peptide-receptor specificity within the ghrelin signaling axis.
Peptide signaling pathway analysis: The compound serves as a selective probe for investigating signaling pathways triggered by non-acylated ghrelin forms. Its inability to activate the canonical ghrelin receptor allows researchers to distinguish receptor-dependent from receptor-independent effects in cellular and tissue models. Utilizing [Des-octanoyl]-Ghrelin in these analyses helps define the spectrum of biological processes influenced by non-acylated peptides, including potential autocrine and paracrine signaling mechanisms that are independent of classical ghrelin receptor activation.
Metabolic function research: Non-acylated ghrelin analogs like [Des-octanoyl]-Ghrelin are essential for exploring the metabolic roles of ghrelin peptides beyond growth hormone release. In rodent studies, this compound enables the investigation of energy balance, glucose metabolism, and adiposity regulation without the confounding influence of receptor-mediated endocrine effects. Such research contributes to a nuanced understanding of ghrelin's diverse physiological functions and facilitates the identification of novel metabolic pathways modulated by peptide derivatives.
Peptide structure-activity relationship (SAR) studies: The distinct lack of octanoylation in [Des-octanoyl]-Ghrelin makes it a key reference compound for SAR investigations. By systematically comparing the biological activities of acylated and non-acylated ghrelin peptides, scientists can pinpoint the structural features critical for function, receptor interaction, and downstream signaling. These insights are valuable for the rational design of new peptide analogs with tailored biological properties for advanced biochemical research.
Analytical method development: The peptide is also utilized as a standard or control in the development and validation of analytical methods for peptide quantification and characterization. Its unique mass and chromatographic properties, relative to acylated ghrelin, make it suitable for calibrating detection systems, optimizing separation protocols, and establishing specificity in assays designed to distinguish between different ghrelin isoforms. This application ensures robust and reliable measurement of peptide species in complex biological matrices, supporting high-quality biochemical investigations.
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