PHI 27 (human) trifluoroacetate is a peptide containing a blend of polar, aromatic, and basic residues that contribute to extended conformational variability. Researchers employ it to explore receptor-contact motifs, helical propensity, and solvent-driven folding. The TFA form enhances solubility and purification robustness. Its composition supports thorough structural studies.
CAT No: R2207
CAS No:2828433-29-8
Synonyms/Alias:PHI 27 (human) trifluoroacetate;EX-A7137;2828433-29-8;
PHI 27 (human) trifluoroacetate is a synthetic peptide corresponding to the human pancreatic polypeptide hormone PHI 27, also known as peptide histidine isoleucine. As a member of the vasoactive intestinal peptide (VIP)/secretin/glucagon family, PHI 27 plays a significant role in the regulation of gastrointestinal and pancreatic functions. The trifluoroacetate salt form ensures enhanced solubility and stability, making it suitable for a range of in vitro and in vivo research applications. Its unique sequence and biological activity have made it a valuable tool for investigating peptide signaling pathways, receptor interactions, and neuroendocrine regulation in both fundamental and applied biomedical research.
Receptor binding studies: PHI 27 is commonly employed as a ligand in receptor binding assays aimed at characterizing the specificity and affinity of peptide receptors, particularly those related to the VIP/PACAP receptor family. By facilitating the mapping of receptor distribution and elucidating ligand-receptor interactions, PHI 27 enables researchers to dissect the molecular mechanisms underlying peptide-mediated signaling in neural and gastrointestinal tissues. Such studies are instrumental in advancing the understanding of G protein-coupled receptor (GPCR) pharmacology and the broader field of peptide-receptor biology.
Signal transduction research: The peptide serves as a model agonist for probing intracellular signaling cascades initiated by peptide hormone receptors. Researchers utilize PHI 27 to stimulate target cells and monitor downstream effects such as cyclic AMP (cAMP) production, calcium mobilization, and kinase activation. These experimental approaches provide insights into the physiological roles of peptide hormones, help clarify the cross-talk between signaling pathways, and offer a platform for screening potential modulators or inhibitors of peptide-induced responses.
Neuroendocrine function analysis: PHI 27 is a valuable investigative tool for examining neuroendocrine regulation, particularly in studies of the enteric nervous system and pancreatic islet biology. Its ability to mimic endogenous peptide activity allows for the assessment of hormone release, neurotransmitter modulation, and the integration of neural and endocrine signals. Experimental models employing PHI 27 have contributed to the understanding of peptide-mediated control of gastrointestinal motility, secretion, and metabolic regulation.
Peptide structure-activity relationship (SAR) studies: The defined sequence and biological activity of PHI 27 make it suitable for SAR investigations aimed at identifying critical residues responsible for receptor activation and specificity. Researchers can employ this peptide as a reference compound to compare the activity of analogs, truncated variants, or modified peptides. Such studies are essential for rational peptide design, optimization of bioactivity, and the development of novel peptide-based research tools.
Peptide synthesis and analytical standard: Due to its well-characterized structure, PHI 27 is frequently used as a reference standard in peptide synthesis validation and quality control protocols. Analytical laboratories employ it to calibrate chromatographic systems, verify peptide purity, and optimize mass spectrometric detection methods. Its reproducibility and defined physicochemical properties support reliable benchmarking in peptide production workflows, ensuring consistency in research and development settings.
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