Substance P(1-7) (TFA) constitutes the N-terminal segment of Substance P, retaining key aromatic and basic residues that influence structural dynamics. Researchers use it to examine peptide-protein interfaces, β-turn formation, and solvent effects. The sequence provides insight into truncated peptide behavior. The TFA form allows predictable solvation for assays.
CAT No: R2205
CAS No:2828433-22-1
Synonyms/Alias:Substance P(1-7) (TFA);Substance P(1-7) TFA;2828433-22-1;(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-1-[(2S)-2-amino-5-(diaminomethylideneamino)pentanoyl]pyrrolidine-2-carbonyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoic acid;2,2,2-trifluoroacetic acid;1-7-Substance P trifluoroacetate;HY-P1485A;MS-31866;CS-0046306;G16494;
Substance P(1-7) (TFA) is a synthetic peptide fragment corresponding to the N-terminal sequence of the neuropeptide Substance P, comprising amino acids 1 through 7 and typically supplied as the trifluoroacetate salt. As a biologically relevant peptide derivative, it serves as a valuable research tool for dissecting the structure-function relationships and receptor interactions of tachykinin family members. The truncated form retains key functional motifs present in the parent molecule, enabling researchers to investigate the specific contributions of the N-terminal region to biological activity, receptor binding, and downstream signaling pathways. Its well-defined sequence and stability in aqueous environments make it particularly suitable for controlled experimental studies in neurobiology, peptide pharmacology, and cell signaling research.
Peptide receptor interaction studies: As a defined fragment of Substance P, this peptide is widely used to probe the binding specificity and functional roles of neurokinin receptors, particularly the NK1 receptor. By comparing the activity of the 1-7 fragment to that of the full-length peptide, researchers can delineate the minimal structural requirements for receptor engagement and activation. Such studies are instrumental in mapping receptor binding domains, understanding ligand-receptor dynamics, and developing selective receptor modulators for basic research purposes.
Neurobiology research: The 1-7 fragment is frequently employed to investigate the physiological and biochemical roles of Substance P in the central and peripheral nervous systems. Its application allows for the selective assessment of N-terminal-mediated effects, such as modulation of neurotransmitter release, neuronal excitability, and synaptic plasticity. By isolating the actions of this specific region, scientists can better understand the mechanisms underlying pain transmission, neurogenic inflammation, and stress responses, contributing to the broader field of neuropeptide function.
Peptide structure-activity relationship (SAR) analysis: Substance P(1-7) (TFA) is a critical tool in SAR studies, where systematic modifications of peptide fragments reveal the influence of sequence and conformation on biological activity. By incorporating this fragment into comparative assays, researchers can identify which residues and structural motifs are essential for bioactivity, receptor selectivity, or enzymatic stability. These insights inform the rational design of novel peptide analogs and help elucidate the molecular determinants of tachykinin family function.
Enzymatic degradation and metabolism assays: The 1-7 fragment is often utilized in studies of peptide metabolism, serving as a substrate for peptidases and proteases that process tachykinin peptides. Monitoring the degradation kinetics and metabolic fate of this fragment provides valuable information on the regulatory pathways controlling neuropeptide turnover in biological systems. Such data are essential for understanding how peptide fragments are generated in vivo and how their persistence or clearance affects physiological signaling.
Peptide synthesis and analytical method development: In peptide chemistry, Substance P(1-7) (TFA) serves as a reference standard and model compound for optimizing solid-phase peptide synthesis protocols, purification strategies, and analytical characterization techniques. Its defined sequence and physicochemical properties make it suitable for calibrating chromatographic systems, validating mass spectrometry methods, and assessing the efficiency of peptide assembly. These applications support the advancement of peptide synthesis methodologies and quality control practices in both academic and industrial laboratories.
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