Octreotide trifluoroacetate salt (Dimer, Parallel) forms a structured peptide assembly valuable for conformational and multimerization research. Parallel dimerization enhances studies of intermolecular stability and cooperative binding. The trifluoroacetate counterion contributes to solubility and purification behavior. Research fields include peptide hormone analog development, structural modeling, and receptor-interaction studies.
CAT No: R2301
CAS No:1926163-80-5
Synonyms/Alias:1926163-80-5;Octreotide trifluoroacetate salt (Dimer, Parallel);MFCD30748663;
Octreotide trifluoroacetate salt (Dimer, Parallel) is a synthetic peptide analog of somatostatin, engineered to exhibit enhanced stability and biological activity compared to the native hormone. Characterized by its dimeric, parallel configuration, this compound is notable for its capacity to modulate multiple signaling pathways through high-affinity binding to somatostatin receptors. Its unique structural features, including the presence of the trifluoroacetate counterion and parallel dimerization, make it a valuable tool for probing peptide-receptor interactions and elucidating mechanisms of peptide-based regulation in complex biological systems. As a chemically defined peptide, it serves as a critical resource for researchers investigating peptide structure-function relationships, receptor pharmacology, and the development of next-generation peptide-based technologies.
Receptor Binding Studies: The dimeric form of octreotide is particularly advantageous for in vitro assays aimed at characterizing somatostatin receptor binding kinetics and affinity profiles. Its parallel configuration allows for the simultaneous engagement of multiple receptor sites, facilitating the investigation of receptor dimerization, allosteric modulation, and signal transduction mechanisms. Researchers employ this compound to dissect the molecular determinants of peptide-receptor specificity and to map critical residues involved in ligand recognition, providing foundational insights for rational drug design and receptor-targeted screening platforms.
Peptide Structure-Activity Relationship (SAR) Analysis: The parallel dimeric structure of this peptide enables detailed studies into the impact of multivalency and spatial arrangement on biological activity. By comparing the activity profiles of monomeric versus dimeric and parallel versus antiparallel arrangements, scientists can delineate the structural features that govern potency, selectivity, and receptor subtype preference. Such SAR investigations are instrumental in guiding the optimization of peptide therapeutics, imaging agents, and molecular probes for research applications.
Peptide Synthesis and Method Development: As a model system, the parallel dimer serves as a benchmark for validating advanced solid-phase peptide synthesis (SPPS) techniques and optimizing conjugation strategies. Its defined architecture provides a robust test case for assessing the efficiency of dimerization protocols, the stability of peptide linkages, and the compatibility of protecting group strategies. Synthetic chemists utilize it to refine methodologies for producing complex peptide assemblies, which are increasingly important in the fields of chemical biology and biomaterials research.
Analytical Method Validation: The physicochemical properties of the dimeric peptide, including its chromatographic behavior and mass spectral profile, make it suitable for use as a standard in the development and validation of analytical techniques. Laboratories leverage this compound to calibrate and troubleshoot high-performance liquid chromatography (HPLC), mass spectrometry (MS), and capillary electrophoresis (CE) methods tailored for peptide detection and quantification. Its consistent performance supports reliable quality control and reproducibility in peptide analysis workflows.
Biophysical Interaction Studies: The parallel dimer format is well-suited for investigating the fundamental principles of peptide self-association, aggregation, and intermolecular interactions. These studies are essential for understanding the physicochemical parameters that influence peptide solubility, stability, and higher-order assembly in solution. Such knowledge underpins the rational design of peptide-based nanomaterials, delivery systems, and scaffolds with tailored functional properties for advanced research and development initiatives.
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5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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