N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH presents a complex multi-residue architecture containing D/L stereochemistry and heterocyclic modifications. The abundant diversity of hydrophobic, aromatic, and acidic residues shapes a dynamic conformational landscape. Researchers use it to explore folding pathways, charge distribution, and binding equilibria. Applications extend to peptide engineering, structural analysis, and sequence-function correlation studies.
CAT No: R2457
CAS No:133658-45-4
Synonyms/Alias:N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH;133658-45-4;N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH;
N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH is a complex synthetic peptide featuring a diverse sequence of amino acids, including several D- and L- isomers, as well as unique modifications such as imidazolyl groups. This intricate molecular architecture imparts the compound with distinct physicochemical properties, making it highly valuable for advanced research in peptide chemistry and molecular biology. Its sequence allows for the investigation of stereochemical effects, conformational dynamics, and functional group interactions within peptide chains. The presence of both hydrophilic and hydrophobic residues, along with aromatic and charged side chains, provides a versatile platform for studying a wide range of biochemical processes and molecular recognition events.
Peptide Structure-Activity Relationship Studies: N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH serves as a robust model for exploring how sequence variations and stereochemistry influence peptide structure and biological activity. Researchers utilize this compound to systematically analyze the impact of D- versus L- amino acids, the role of aromatic and imidazolyl modifications, and the effect of sequence positioning on peptide folding and function. Such studies are critical for developing new synthetic peptides with tailored properties for biochemical assays, molecular probes, or as leads in drug discovery.
Enzyme Substrate Specificity Analysis: The unique sequence and modifications present in this peptide make it a valuable substrate for investigating enzyme specificity, particularly for proteases and peptidases. By incorporating both standard and non-standard amino acids, as well as imidazolyl functional groups, the compound enables the assessment of enzyme recognition patterns, cleavage sites, and catalytic preferences. This application is essential for elucidating enzyme mechanisms and for designing inhibitors or substrates with enhanced selectivity and stability in enzymology research.
Receptor Binding and Interaction Studies: The multifaceted nature of this synthetic peptide allows it to be employed in receptor binding assays, where its diverse side chains facilitate the exploration of peptide-receptor interactions. Scientists can probe the influence of specific residues or modifications on binding affinity, selectivity, and conformational changes upon receptor engagement. These insights are pivotal for mapping binding epitopes, understanding signal transduction pathways, and developing peptide-based ligands for research purposes.
Peptide-Based Material Science: Due to its unique combination of amino acids and structural motifs, this compound finds application in the development of peptide-based materials and nanostructures. Its sequence can be leveraged to investigate self-assembly, aggregation behavior, and the formation of supramolecular architectures. Such research supports the creation of novel biomaterials with tunable properties for use in biosensing, drug delivery systems, or as scaffolds in tissue engineering.
Analytical Method Development: N(1)Gly-DL-Phe-DL-xiIle-Gly-DL-Trp-Gly-DL-Asn-DL-Asp(1)-DL-xiIle-DL-Phe-Gly-DL-Ala(imidazol-2-yl)(imidazol-2-yl)-DL-Tyr-DL-Ser-Gly-DL-Asp-DL-Phe-OH is frequently utilized as a challenging analyte for the validation and optimization of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its complex sequence, stereochemical diversity, and presence of non-standard residues provide a rigorous test for method sensitivity, resolution, and accuracy. This application is vital for laboratories developing new protocols for peptide analysis, quantification, and characterization in research and quality control settings.
3. TMEM16F and dynamins control expansive plasma membrane reservoirs
4. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
5. SERS spectrum of the peptide thymosin‐β4 obtained with Ag nanorod substrate
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