Octreotide acetate is a longer acting synthetic octapeptide analog of naturally occurring somatostatin. It inhibits the secretion of gastro-entero-pancreatic peptide hormones and the release of growth hormone.
CAT No: 10-101-199
N-Acetyl-Phe-Octreotide is a synthetic peptide analog structurally related to somatostatin, designed to enhance stability and bioactivity in biochemical research settings. Featuring an N-acetylated phenylalanine at its N-terminus, this compound exhibits unique conformational properties that influence its interaction with somatostatin receptors and related signaling pathways. Its engineered sequence and chemical modifications confer increased resistance to enzymatic degradation, making it a valuable tool for probing peptide-receptor dynamics, investigating peptide stability, and supporting the development of novel peptide-based agents. As a research-use-only compound, it is widely recognized for its role in advancing the understanding of peptide structure-activity relationships and receptor selectivity in both academic and industrial laboratories.
Receptor binding studies: N-Acetyl-Phe-Octreotide is frequently employed in receptor binding assays to elucidate the affinity and specificity of somatostatin analogs for their respective G protein-coupled receptors (GPCRs). The N-terminal acetylation and phenylalanine substitution can modulate receptor interaction profiles, allowing researchers to systematically analyze the impact of sequence modifications on ligand-receptor recognition. Such studies contribute to the mapping of critical binding motifs and inform the rational design of next-generation peptide ligands with tailored pharmacological profiles.
Peptide stability analysis: Due to its enhanced resistance to proteolytic cleavage, this analog serves as an ideal substrate for investigating peptide stability in biological matrices, including plasma and tissue homogenates. Researchers utilize it to assess degradation kinetics, identify metabolic cleavage sites, and compare the stability of modified versus native peptide sequences. Insights gained from these experiments guide the optimization of peptide therapeutics and diagnostic agents with improved in vivo half-life and functional persistence.
Structure-activity relationship (SAR) investigations: The distinct sequence and chemical modifications present in N-Acetyl-Phe-Octreotide make it a critical reference compound in SAR studies. By comparing its biological and physicochemical properties with those of related analogs, scientists can delineate the contributions of individual amino acid residues and terminal modifications to overall peptide activity. These findings are instrumental in guiding the design of new analogs with enhanced selectivity, potency, or stability.
Peptide synthesis optimization: The compound is also utilized as a model substrate for refining solid-phase peptide synthesis methodologies. Its sequence complexity and post-synthetic modifications provide a robust test case for evaluating coupling efficiency, protecting group strategies, and purification protocols. Results from such optimization efforts can be extrapolated to the synthesis of other challenging peptide targets, thus streamlining workflow and improving overall yield and purity in research and industrial peptide production.
Analytical method development: N-Acetyl-Phe-Octreotide is employed as a reference standard or test analyte in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized structure and stability make it suitable for calibrating instrumentation, optimizing chromatographic conditions, and establishing detection limits for peptide-based samples. These analytical advances are essential for ensuring the quality and reproducibility of peptide research and production processes.
1. High fat diet and GLP-1 drugs induce pancreatic injury in mice
2. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
4. Cationic cell-penetrating peptides are potent furin inhibitors
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