Octreotide-phenylalanine-d8 di-Trifluoroacetic Acid Salt

Octreotide-phenylalanine-d8 di-Trifluoroacetic Acid Salt is a synthetic peptide analog of somatostatin, uniquely labeled with deuterated phenylalanine residues and provided as a di-trifluoroacetic acid salt. Its structure combines the established bioactivity of octreotide with stable isotope labeling, making it a valuable tool in peptide research and analytical biochemistry. The presence of deuterium atoms enhances its utility in mass spectrometric applications, while the peptide backbone preserves key functional motifs for receptor interaction studies. This compound is particularly relevant for researchers investigating peptide pharmacokinetics, receptor binding mechanisms, and advanced analytical workflows requiring precise molecular tracing.

Quantitative Mass Spectrometry: In proteomics and bioanalytical chemistry, the deuterium-labeled octreotide variant serves as an internal standard for quantitative mass spectrometry. The incorporation of phenylalanine-d8 enables clear distinction from endogenous or unlabeled analogs, facilitating accurate quantification of octreotide or related peptides in complex biological samples. By providing a stable isotope signature, it helps correct for sample preparation variability and instrument response, thereby improving the reliability of pharmacokinetic and biodistribution studies.

Peptide Metabolism Studies: The labeled peptide is highly suited for detailed investigations of peptide metabolism and degradation pathways. Researchers can use it to track metabolic fate, identify cleavage products, and elucidate enzymatic processing in vitro or in cell-based systems. The deuterium labeling allows for unambiguous differentiation of the administered compound from naturally occurring peptides, supporting mechanistic studies on peptide stability, enzymatic specificity, and metabolic turnover.

Receptor Binding Assays: As an analog of somatostatin, octreotide derivatives are widely used to explore receptor-ligand interactions, particularly with somatostatin receptor subtypes. The deuterated version enables parallel binding studies alongside unlabeled peptides, offering insights into receptor affinity, selectivity, and functional modulation. By using isotopically labeled standards, researchers can achieve higher confidence in competitive binding assays and receptor characterization protocols.

Peptide Synthesis and Analytical Method Development: The compound's precise isotopic labeling makes it a valuable reference material in the development and validation of peptide synthesis protocols. It can be used to assess synthetic yield, monitor purification efficiency, and optimize analytical detection methods such as HPLC and LC-MS. Its well-defined mass shift facilitates calibration and troubleshooting in analytical workflows involving structurally related peptides.

Pharmacokinetic Profiling: Stable isotope-labeled peptides are essential in non-clinical pharmacokinetic studies, enabling the assessment of absorption, distribution, metabolism, and excretion properties without interference from endogenous analogs. The deuterium-labeled octreotide variant supports time-course studies, tissue distribution analysis, and bioanalytical validation, providing robust data for preclinical research and peptide drug development pipelines. By leveraging its unique labeling, researchers can obtain high-precision kinetic profiles and enhance the interpretive power of their experimental results.

1. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists

2. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis

3. Myotropic activity and immunolocalization of selected neuropeptides of the burying beetle Nicrophorus vespilloides (Coleoptera: Silphidae)

4. An Isolated TCR αβ Restricted by HLA-A* 02: 01/CT37 Peptide Redirecting CD8+ T Cells to Kill and Secrete IFN-γ in Response to Lung Adenocarcinoma Cell Lines

5. Characterization of Novel P-Selectin Targeted Complement Inhibitors in Murine Models of Hindlimb Injury and Transplantation