Ntfapi

Ntfapi presents a peptide scaffold containing varied functional groups that drive diverse folding states and solubility patterns. Researchers analyze hydrogen-bonding tendencies and charge distribution. Its conformational adaptability aids interaction profiling. Applications span ligand design, structural exploration, and peptide optimization.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Ntfapi(CAS 2374782-03-1)

CAT No: R2536

CAS No:2374782-03-1

Synonyms/Alias:NTFAPI;NOTA-FAPI;2374782-03-1;NOTA-FAPI-04;RD4ZKJ67G3;FAPI-42;(S)-2,2'-(7-(2-(4-(3-((4-((2-(2-Cyano-4,4-difluoropyrrolidin-1-yl)-2-oxoethyl)carbamoyl)quinolin-6-yl)oxy)propyl)piperazin-1-yl)-2-oxoethyl)-1,4,7-triazonane-1,4-diyl)diacetic acid;1H-1,4,7-Triazonine-1,4(5H)-diacetic acid, 7-(2-(4-(3-((4-(((2-((2S)-2-cyano-4,4-difluoro-1-pyrrolidinyl)-2-oxoethyl)amino)carbonyl)-6-quinolinyl)oxy)propyl)-1-piperazinyl)-2-oxoethyl)hexahydro-;1H-1,4,7-Triazonine-1,4(5H)-diacetic acid, 7-[2-[4-[3-[[4-[[[2-[(2S)-2-cyano-4,4-difluoro-1-pyrrolidinyl]-2-oxoethyl]amino]carbonyl]-6-quinolinyl]oxy]propyl]-1-piperazinyl]-2-oxoethyl]hexahydro-;UNII-RD4ZKJ67G3;SCHEMBL21257092;XQARGGQZFNOLDH-SANMLTNESA-N;EX-A4616;AT43727;HY-136641;CS-0132761;2-[4-(carboxymethyl)-7-[2-[4-[3-[4-[[2-[(2S)-2-cyano-4,4-difluoropyrrolidin-1-yl]-2-oxoethyl]carbamoyl]quinolin-6-yl]oxypropyl]piperazin-1-yl]-2-oxoethyl]-1,4,7-triazonan-1-yl]acetic acid;

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M.F/Formula
C36H47F2N9O8
M.W/Mr.
771.8

Ntfapi, also known as N-terminal formylated alanine-proline-isoleucine, is a synthetic peptide compound that serves as a molecular tool in the study of innate immune signaling and cell migration. Characterized by its N-terminal formyl group, Ntfapi mimics naturally occurring formyl peptides that are recognized by formyl peptide receptors (FPRs) on the surface of various immune cells. This structural property makes it a valuable probe for dissecting receptor-ligand interactions, elucidating chemotactic mechanisms, and modeling inflammatory processes in vitro. Its defined sequence and chemical stability allow for reproducible experimentation in both basic and applied peptide research.

Chemotaxis research: Ntfapi is widely utilized in the investigation of chemotactic responses, particularly those mediated by neutrophils and monocytes. By acting as a high-affinity ligand for formyl peptide receptors, it enables researchers to stimulate and quantify directed cell migration in response to specific molecular cues. This application is crucial for unraveling the signaling pathways that govern immune cell trafficking, understanding the molecular basis of inflammation, and identifying potential modulators of chemotactic activity.

Receptor binding studies: As a structurally defined formylated peptide, Ntfapi serves as a model ligand in binding assays aimed at characterizing the specificity, affinity, and activation profiles of FPR family receptors. Its use in radioligand displacement, fluorescence polarization, and surface plasmon resonance assays provides detailed insights into receptor-ligand interactions, conformational changes upon binding, and downstream signal transduction events. Such studies are vital for the rational design of receptor-targeted probes and for advancing knowledge of innate immune recognition.

Signal transduction analysis: Ntfapi facilitates the exploration of intracellular signaling cascades triggered by FPR engagement. By applying this peptide to cultured immune cells, researchers can monitor activation of key pathways, such as calcium mobilization, MAP kinase phosphorylation, and G-protein-coupled signaling events. These analyses help delineate the molecular mechanisms underlying immune cell activation and provide a controlled context for testing the effects of pathway inhibitors or genetic modifications.

Inflammatory modeling: The peptide is employed in in vitro models that replicate aspects of acute and chronic inflammation. Through its ability to induce chemotactic and activation responses in leukocytes, it supports the development of experimental systems for studying the recruitment and function of immune cells under inflammatory conditions. Such models are instrumental for screening anti-inflammatory compounds, investigating the dynamics of immune cell infiltration, and probing the interplay between different cell types during immune responses.

Peptide structure-activity relationship (SAR) studies: Ntfapi's well-defined sequence and modifiable structure make it a useful scaffold for SAR investigations. By systematically altering amino acid residues or chemical modifications, researchers can assess the impact of structural changes on receptor affinity, biological activity, and stability. These studies contribute to the optimization of peptide ligands for research applications, enhance understanding of peptide-receptor interactions, and inform the design of novel bioactive molecules for experimental use.

InChI
InChI=1S/C36H47F2N9O8/c37-36(38)19-26(20-39)47(25-36)31(48)21-41-35(54)28-4-5-40-30-3-2-27(18-29(28)30)55-17-1-6-42-13-15-46(16-14-42)32(49)22-43-7-9-44(23-33(50)51)11-12-45(10-8-43)24-34(52)53/h2-5,18,26H,1,6-17,19,21-25H2,(H,41,54)(H,50,51)(H,52,53)/t26-/m0/s1
InChI Key
XQARGGQZFNOLDH-SANMLTNESA-N

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