Irucalantide is a peptide analog with aromatic and charged residues that create distinct conformational states. Researchers use it to examine β-turn formation, backbone flexibility, and peptide-protein recognition. The sequence supports folding analyses under varied solvent conditions. Its architecture suits comprehensive biophysical evaluation.
CAT No: R2501
CAS No:1631160-47-8
Synonyms/Alias:Irucalantide;1631160-47-8;irucalantide [INN];OV42G2O3SQ;HY-P5536;DA-54386;CS-0886413;L-Cysteinamide, N-acetyl-S-[[3,5-bis(mercaptomethyl)phenyl]methyl]-L-cysteinyl-L-seryl-L-phenylalanyl-(2S)-2-azetidinecarbonyl-L-tyrosyl-N6-(aminoiminomethyl)-L-lysyl-L-cysteinyl-L-alanyl-psi(CH2-NH)-L-histidyl-L-glutaminyl-L-alpha-aspartyl-L-leucyl-, cyclic (1-->7),(1-->13)-bis(thioether);
Irucalantide, also known as a synthetic peptide analog, represents a significant advancement in the realm of carbohydrate compounds and peptide-based research. Engineered to mimic the structure and function of naturally occurring peptide hormones, Irucalantide is characterized by its stability and bioactivity, making it a valuable tool in various scientific disciplines. Its unique sequence and conformational properties allow for targeted interactions with specific receptors, facilitating precise modulation of biological pathways. Researchers are increasingly turning to Irucalantide for its versatility in experimental design and its ability to yield reproducible, reliable results in both in vitro and in vivo settings.
Pharmacological mechanism studies: Irucalantide serves as a powerful model compound for elucidating the mechanisms of peptide-receptor interactions. By incorporating this peptide into receptor binding assays or cell signaling studies, scientists can investigate the nuances of receptor activation, downstream signaling cascades, and feedback regulation. Its well-defined structure enables detailed mapping of binding sites and conformational changes, providing insights that are crucial for the rational design of new therapeutic agents and for understanding the fundamental principles of peptide hormone action.
Peptide drug development: As a synthetic analog, Irucalantide is frequently utilized in the early stages of peptide drug discovery and optimization. Its robust pharmacokinetic profile and resistance to enzymatic degradation make it an excellent candidate for structure-activity relationship (SAR) studies. Researchers employ it to test modifications that enhance stability, bioavailability, or receptor selectivity, paving the way for the development of next-generation peptide therapeutics. The data generated from such studies inform the design of analogs with improved efficacy and safety profiles, ultimately accelerating the pipeline from bench to preclinical research.
Biochemical assay development: In the context of biochemical assays, Irucalantide is often used as a reference peptide or positive control. Its predictable activity and well-characterized properties allow assay developers to validate new detection methods, calibrate analytical instruments, and establish baseline responses for comparative studies. It plays a critical role in the standardization of protocols, ensuring consistency across different laboratories and experimental setups. The availability of such a reliable peptide standard streamlines assay development and increases the reproducibility of experimental outcomes.
Receptor selectivity profiling: Irucalantide is a valuable tool in profiling the selectivity of peptide ligands for various receptor subtypes. By systematically assessing its binding affinity and functional activity across a panel of related receptors, researchers can delineate the specificity and cross-reactivity of peptide-receptor interactions. This information is essential for identifying off-target effects, optimizing lead compounds, and advancing the understanding of receptor pharmacology. The ability to differentiate subtle differences in receptor engagement contributes to the refinement of therapeutic strategies targeting peptide hormone pathways.
Structure-function relationship research: The distinct sequence and conformational features of Irucalantide make it an ideal subject for studies aimed at deciphering structure-function relationships in peptides. Using techniques such as NMR spectroscopy, X-ray crystallography, or molecular modeling, scientists can correlate specific structural motifs with biological activity. These investigations shed light on the determinants of receptor recognition, signal transduction, and functional selectivity, providing a foundation for rational peptide engineering. Insights gained from such studies not only inform the design of novel analogs but also enhance the broader understanding of peptide biology and its applications in biomedical research.
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