F-992 presents a specialized peptide-derived framework used to analyze receptor-binding determinants and conformational behavior. Varied residue chemistry shapes interactions between hydrophobic and charged domains. Researchers employ it to probe structural constraints and binding equilibria. Broad applications include ligand-optimization studies, sequence refinement, and bioactive peptide modeling.
CAT No: R2502
CAS No:162277-99-8
Synonyms/Alias:F992;N39Q2H8V0B;162277-99-8;F-992;UNII-N39Q2H8V0B;(D-Phe2, THI3,a-me-abu4, HYP7, D-Arg8)-dc1-vasopressin;Glycinamide, N-(4-mercapto-1-oxobutyl)-D-phenylalanyl-3-(2-thienyl)-L-alanyl-L-isovalyl-L-asparaginyl-L-cysteinyl-(4R)-4-hydroxy-L-prolyl-D-arginyl-, cyclic (1->5)-thioether;DTXSID401026273;HY-P0041;DA-73287;CS-0014970;(2S,4R)-N-[(2R)-1-[(2-amino-2-oxoethyl)amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]-1-[(3R,6S,9S,12S,15R)-6-(2-amino-2-oxoethyl)-15-benzyl-9-ethyl-9-methyl-5,8,11,14,17-pentaoxo-12-(thiophen-2-ylmethyl)-1-thia-4,7,10,13,16-pentazacycloicosane-3-carbonyl]-4-hydroxypyrrolidine-2-carboxamide;Glycinamide, N-(4-mercapto-1-oxobutyl)-D-phenylalanyl-3-(2-thienyl)-L-alanyl-L-isovalyl-L-asparaginyl-L-cysteinyl-(4R)-4-hydroxy-L-prolyl-D-arginyl-, cyclic (1-->5)-thioether;Glycinamide, N-(4-mercapto-1-oxobutyl)-D-phenylalanyl-3-(2-thienyl)-L-alanyl-L-isovalyl-L-asparaginyl-L-cysteinyl-(4R)-4-hydroxy-L-prolyl-D-arginyl-, cyclic (1a5)-thioether;
F-992 is a specialized carbohydrate compound known for its unique structural characteristics and versatile reactivity, making it highly valuable in a range of biochemical and analytical research applications. As a member of the oligosaccharide family, F-992 exhibits notable solubility and stability under typical laboratory conditions, facilitating its integration into various experimental workflows. Its molecular architecture allows for selective interactions with proteins, enzymes, and other biomolecules, thus providing researchers with a reliable tool for probing carbohydrate-mediated processes. The compound's compatibility with diverse analytical techniques further enhances its appeal, supporting its use in both fundamental and applied scientific studies. Researchers appreciate the batch-to-batch consistency and reproducibility that F-992 offers, ensuring dependable results across a spectrum of investigative pursuits.
Glycobiology Research: F-992 is widely utilized in glycobiology research for elucidating carbohydrate-protein interactions, which are pivotal in understanding cellular communication and signaling pathways. By serving as a model substrate or ligand, it enables scientists to dissect the specificity and affinity of lectins, antibodies, and other carbohydrate-binding proteins. These studies contribute to the broader comprehension of cell surface recognition events, immune responses, and pathogen-host interactions. The compound's well-defined structure supports the generation of quantitative binding data and facilitates the mapping of glycan recognition motifs, advancing the field of glycoscience.
Enzyme Substrate Analysis: In the context of enzymology, F-992 functions as an effective substrate for characterizing glycosidase and glycosyltransferase activities. Researchers employ it to monitor enzymatic cleavage or modification, allowing for kinetic studies and the determination of enzyme specificity. The use of F-992 in these assays aids in the identification of novel enzymes and the optimization of biocatalytic processes. Its clear reaction endpoints and compatibility with spectroscopic or chromatographic detection methods streamline the workflow for high-throughput screening and mechanistic enzymology investigations.
Analytical Standards Development: Due to its defined composition, F-992 serves as a reliable analytical standard in carbohydrate quantification and structural elucidation. Laboratories employ it to calibrate instruments such as HPLC, MS, and NMR, ensuring accuracy in the measurement and identification of unknown carbohydrates in complex mixtures. The availability of such a standard enhances method development, validation, and inter-laboratory comparability, supporting robust quality control and research reproducibility.
Vaccine and Antigen Design: The structural motifs present in F-992 render it a valuable component in the design and evaluation of synthetic vaccines or diagnostic antigens. By mimicking naturally occurring glycan epitopes, it can be incorporated into conjugate constructs to investigate immune recognition and antibody binding. This approach aids in the rational development of glycan-based immunogens and diagnostic assays, providing insights into antigenicity and specificity without reliance on animal-derived materials.
Biomaterials Engineering: F-992 is increasingly explored in biomaterials engineering for its potential to modulate cell-surface interactions and material biocompatibility. Incorporation of the carbohydrate moiety into polymeric matrices or surface coatings can influence cell adhesion, proliferation, and differentiation. Researchers utilize these properties to design advanced scaffolds for tissue engineering, biosensors, and drug delivery systems, leveraging the biological functionality imparted by the oligosaccharide structure to create innovative biomedical devices and platforms.
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