Urechistachykinin I

Urechistachykinin I (Uru-TK I), an invertebrate tachykinin-related peptides (TRPs) isolated from echiuroid worms, shows antimicrobial activities without a hemolytic effect.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.

CAT No: R1736

CAS No:149097-03-0

Synonyms/Alias:Uru-TK I

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M.F/Formula
C₅₀H₈₅N₁₉O₁₄
M.W/Mr.
1176.33
Sequence
One Letter Code: LRQSQFVGSR-NH2
three Letter Code: Leu-Arg-Gln-Ser-Gln-Phe-Val-Gly-Ser-Arg-NH2

Urechistachykinin I is a naturally occurring neuropeptide first identified in the marine worm Urechis unicinctus, recognized for its structural similarity to the tachykinin family of peptides. As a biologically active peptide, it features a conserved C-terminal motif that is characteristic of tachykinins, which are known to modulate neurotransmission, smooth muscle contraction, and a variety of physiological processes across diverse animal taxa. The distinctive sequence and functional properties of Urechistachykinin I make it a valuable molecular tool for researchers investigating the evolution, signaling mechanisms, and functional diversity of neuropeptides in invertebrates and comparative physiology.

Peptide receptor characterization: Urechistachykinin I serves as a robust ligand for probing tachykinin receptor subtypes in invertebrate systems. By applying this peptide in receptor binding assays and cell-based signaling studies, researchers can delineate the pharmacological properties, binding affinities, and downstream signaling cascades associated with tachykinin-like receptors. This enables a detailed understanding of receptor-ligand specificity and supports the identification of novel receptor isoforms or subfamilies in non-mammalian species.

Comparative neurobiology: The unique origin and structure of Urechistachykinin I facilitate comparative studies of neuropeptide evolution and function. Utilizing this peptide in cross-species analyses allows scientists to investigate the conservation and divergence of tachykinin signaling pathways, shedding light on the molecular evolution of neuropeptidergic systems. These insights are instrumental in mapping the phylogenetic relationships among peptide families and elucidating their adaptive significance in different ecological contexts.

Smooth muscle physiology: Functional assays employing Urechistachykinin I provide an effective means to study the contractile responses of invertebrate smooth muscle tissues. By measuring muscle tension or motility changes upon peptide application, investigators can characterize the physiological roles of tachykinin-like peptides in gut motility, reproductive processes, or other organ systems. Such studies contribute to a broader understanding of peptidergic regulation of muscle function in invertebrate models.

Peptide structure-activity relationship (SAR) research: Urechistachykinin I is frequently used as a template for SAR studies aimed at deciphering the relationship between peptide sequence, conformation, and biological activity. Through systematic modification of its amino acid residues or C-terminal motif, researchers can assess the impact on receptor binding and functional potency, advancing the rational design of peptide analogs with tailored properties for experimental or biotechnological applications.

Analytical method development: The well-defined sequence and bioactivity of Urechistachykinin I make it a suitable standard or reference compound for developing and validating analytical methods in peptide research. Techniques such as mass spectrometry, high-performance liquid chromatography (HPLC), and immunoassays can be optimized using this peptide to ensure sensitivity, specificity, and reproducibility in the detection and quantification of tachykinin-like molecules in complex biological samples. These methodological advances support broader studies in neuropeptide profiling and functional genomics.

Length
10

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