Anrikefon presents a peptide-derived scaffold with balanced hydrophobic and polar residues that govern its structural adaptability. The sequence offers a platform for studying binding determinants and charge distribution. Researchers examine its conformational dynamics across solvent environments. Uses include ligand-model development, peptide-design research, and biophysical interaction analysis.
CAT No: R2624
CAS No:2269511-95-5
Synonyms/Alias:Anrikefon;Anrikefon [INN];22SCY98BXV;2269511-95-5;UNII-22SCY98BXV;1-(7-(D-Phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)-2,7-diazaspiro(3.5)non-2-yl)ethanone;1-(7-(D-Phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)- 2,7-diazaspiro(3.5)nonan-2-yl)ethan-1-one;Ethanone, 1-(7-(D-phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)-2,7-diazaspiro(3.5)non-2-yl)-;1-[7-(D-phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)- 2,7-diazaspiro[3.5]nonan-2-yl]ethan-1-one;1-[7-(D-Phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)-2,7-diazaspiro[3.5]non-2-yl]ethanone;Ethanone, 1-[7-(D-phenylalanyl-D-phenylalanyl-D-leucyl-D-lysyl)-2,7-diazaspiro[3.5]non-2-yl]-;CHEMBL5095089;SCHEMBL20669227;GLXC-27229;HY-P3445;DA-70882;CS-0541917;(2R)-N-[(2R)-1-(2-acetyl-2,7-diazaspiro[3.5]nonan-7-yl)-6-amino-1-oxohexan-2-yl]-2-[[(2R)-2-[[(2R)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanamide;
Anrikefon is a synthetic peptide compound that has garnered significant interest within the biochemical research community due to its unique sequence and potential for modulating protein-protein interactions. As a laboratory reagent, it serves as a valuable tool for scientists investigating the structural and functional aspects of peptides, particularly those related to signal transduction, receptor binding, and cellular communication. The distinctive properties of Anrikefon, including its amenability to chemical modification and its defined molecular architecture, make it a versatile candidate for a range of experimental applications in peptide science and molecular biology.
Peptide functional studies: Researchers utilize Anrikefon to explore the mechanisms underlying peptide-mediated biological processes, such as receptor activation and intracellular signaling cascades. By incorporating this compound into in vitro assays or cellular models, scientists can dissect the specific contributions of its amino acid sequence to binding affinity, conformational dynamics, and downstream biological responses. The ability to systematically modify Anrikefon's structure further enables detailed structure-activity relationship (SAR) analyses, advancing the understanding of how subtle sequence variations impact peptide function.
Peptide synthesis and method development: Anrikefon is frequently employed as a reference peptide or model substrate in the development and optimization of solid-phase peptide synthesis (SPPS) protocols. Its defined sequence and known physicochemical characteristics provide an ideal benchmark for evaluating coupling efficiency, resin compatibility, and purification strategies. Methodological advances achieved using this peptide can then be translated to the synthesis of more complex or bioactive sequences, thereby accelerating progress in peptide chemistry and pharmaceutical research.
Analytical assay calibration: In the context of analytical biochemistry, Anrikefon serves as a reliable standard for the calibration and validation of chromatographic, mass spectrometric, or electrophoretic techniques. Its well-characterized properties allow for precise quantification and detection, facilitating the establishment of robust analytical workflows for peptide identification, purity assessment, and quantitation in complex biological samples. The use of such standards is critical for ensuring reproducibility and accuracy in both routine analysis and advanced proteomic investigations.
Protein interaction studies: The compound is also instrumental in probing protein-peptide interactions, which are central to many cellular processes. By acting as a ligand or competitive inhibitor in binding assays, Anrikefon enables the characterization of target protein affinities, specificity profiles, and binding kinetics. These experiments provide valuable insights into the molecular determinants of recognition, informing the design of novel modulators or inhibitors for research applications.
Cellular uptake and stability evaluation: Scientists employ Anrikefon to assess peptide stability and uptake in cellular systems, which are key parameters for evaluating the bioavailability and intracellular delivery of peptide-based agents. Through incubation with cultured cells, it is possible to monitor degradation rates, internalization efficiency, and subcellular localization using various analytical techniques. These studies contribute to the broader understanding of peptide pharmacokinetics and support the rational design of more effective peptide probes and delivery systems for experimental use.
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