PHI 27 features a peptide motif with balanced hydrophobic, polar, and basic residues that influence folding and solubility. Structural flexibility supports studies of receptor interaction and signaling mechanisms. Researchers analyze its domain-level transitions and hydrogen-bonding patterns. Applications span bioactive peptide modeling, structural research, and sequence-function mapping.
CAT No: R2334
CAS No:80458-29-3
Synonyms/Alias:80458-29-3;CID 16132346;PHI 27;L-Isolecucinamide, L-histidyl-L-alanyl-L-alpha-aspartylglycyl-L-valyl-L-phenylalanyl-L-threonyl-L-seryl-L-alpha-aspartyl-L-phenylalanyl-L-seryl-L-arginyl-L-leucyl-L-leucylglycyl-L-glutaminyl-L-leucyl-L-seryl-L-alanyl-L-lysyl-L-lysyl-L-tyrosyl-L-leucyl-L-alpha-glutamyl-L-seryl-L-leucyl-;FP73565;NCGC00167207-01;
PHI 27, also known as Peptide Histidine Isoleucine-27, is a naturally occurring neuropeptide belonging to the glucagon-secretin superfamily. Structurally characterized as a 27-amino-acid peptide, it is widely recognized for its role as a regulatory molecule in neuroendocrine signaling. PHI 27 is endogenously expressed in the gastrointestinal tract and central nervous system, where it modulates a variety of physiological pathways. Its significance in biochemical research stems from its influence on smooth muscle activity, hormone secretion, and neurotransmission, making it a valuable tool for elucidating peptide-mediated signaling mechanisms and receptor interactions.
Peptide receptor characterization: PHI 27 serves as a robust ligand for studying the specificity and function of G protein-coupled receptors (GPCRs), particularly those in the VIP/PACAP receptor family. In vitro and ex vivo assays utilize the peptide to map receptor binding profiles, signal transduction cascades, and downstream cellular responses. Such applications are essential for advancing the understanding of neuropeptide-receptor interactions, supporting both fundamental research and the development of receptor-targeted molecular probes.
Neuroendocrine signaling research: As an endogenous modulator of neuronal and endocrine pathways, PHI 27 is frequently employed to investigate the regulatory networks governing neurotransmitter release and hormonal balance. Experimental models use the peptide to probe its effects on pituitary hormone secretion, enteric nervous system activity, and intercellular communication. These studies contribute to a deeper comprehension of neuropeptide functions in homeostatic regulation and synaptic plasticity.
Smooth muscle physiology: Researchers utilize PHI 27 to examine its modulatory effects on smooth muscle contraction and relaxation, particularly within the gastrointestinal tract. By applying the peptide to tissue preparations or cell cultures, scientists can delineate the molecular mechanisms underlying gut motility, vascular tone, and related physiological processes. This application is instrumental in advancing knowledge of peptide-mediated smooth muscle regulation and its broader implications in organ system function.
Peptide structure-activity relationship (SAR) analysis: The defined sequence and bioactivity of PHI 27 make it an effective model for SAR studies in peptide chemistry. By introducing targeted modifications or synthesizing analogs, researchers can assess the impact of specific residues on receptor affinity, biological activity, and metabolic stability. These investigations inform the design of novel peptides with optimized pharmacological profiles for research use.
Analytical method development: PHI 27 is also utilized as a reference compound in the validation and calibration of analytical techniques such as high-performance liquid chromatography (HPLC) and mass spectrometry. Its well-characterized structure and physicochemical properties make it suitable for optimizing peptide detection, quantification, and purity assessment protocols. This application supports the development of reliable analytical workflows for peptide research and quality control in biochemical laboratories.
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