Substance P (1-7)(TFA) is a fragment of the neuropeptide, substance P (SP). Substance P (1-7)(TFA) gives depressor and bradycardic effects when applied to the nucleus tractus solitarius.
Substance P (1-7)(TFA) is a synthetic peptide fragment derived from the N-terminal sequence of the neuropeptide Substance P, consisting of the first seven amino acids. As a truncated analog, it retains key structural motifs that are critical for receptor interaction studies, while lacking the C-terminal residues associated with full agonist activity. The inclusion of trifluoroacetate (TFA) as a counterion ensures stability and solubility, making this peptide fragment highly suitable for advanced biochemical and pharmacological research. Its relevance spans neurobiology, peptide-receptor interaction studies, and the elucidation of structure-activity relationships within the tachykinin peptide family.
Receptor Binding Studies: Researchers frequently employ the Substance P (1-7) fragment as a tool to dissect the binding requirements and specificity of neurokinin receptors, particularly NK1. By comparing the binding affinities and functional responses of this truncated peptide with those of the full-length Substance P, investigators can identify the minimal sequence elements necessary for effective receptor engagement. Such studies are instrumental in mapping ligand-receptor interfaces and guiding the development of selective receptor modulators.
Structure-Activity Relationship Analysis: The use of this peptide fragment enables detailed examination of the relationship between peptide sequence and biological activity. By systematically substituting or truncating amino acids within the Substance P backbone, scientists can pinpoint residues essential for activity or receptor selectivity. Substance P (1-7) serves as a reference compound in these experiments, providing insights into how N-terminal modifications influence receptor activation and downstream signaling.
Peptide Synthesis and Method Validation: As a well-characterized peptide fragment, Substance P (1-7) is commonly utilized in peptide synthesis laboratories for method development, optimization, and validation. Its defined sequence and physicochemical properties make it an ideal standard for assessing the efficiency of solid-phase peptide synthesis protocols, purification techniques, and analytical methods such as HPLC or mass spectrometry. The fragment's stability and solubility profile further support its use as a calibration or control peptide in various synthetic and analytical workflows.
Neurobiological Research: The truncated peptide is valuable for probing the functional domains of tachykinins in neural signaling. By employing Substance P (1-7) in in vitro assays or cell-based models, researchers can investigate its ability to modulate neuronal activity, neurotransmitter release, or secondary messenger pathways compared to the full-length peptide. These studies contribute to a deeper understanding of the role of Substance P fragments in synaptic transmission and neuropeptide signaling networks.
Peptide-Protein Interaction Studies: In addition to receptor interactions, Substance P (1-7) is used to explore binding with other protein partners, such as enzymes or transporters involved in peptide metabolism. Its truncated structure allows for the identification of binding motifs that are recognized by peptidases or carrier proteins, facilitating investigations into the mechanisms of peptide degradation, clearance, or transport. These insights are essential for advancing knowledge of peptide processing and turnover in biological systems.
1. An Open-label, Single-center, Safety and Efficacy Study of Eyelash Polygrowth Factor Serum
5. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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