Ftisadtsk is a short peptide rich in polar and charged residues that contribute to flexible secondary-structure formation. Researchers employ it to evaluate phosphorylation motifs, residue-specific effects, and solvent-dependent conformational shifts. The sequence supports analysis of peptide-protein interfaces and hydrogen-bonding behavior. Its compact structure provides high analytical versatility.
CAT No: R2268
CAS No:1431957-73-1
Synonyms/Alias:FTISADTSK;1431957-73-1;HY-P3146;AKOS040756800;CS-0149482;(2S)-6-amino-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S,3R)-2-[[(2S)-2-amino-3-phenylpropanoyl]amino]-3-hydroxybutanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxypropanoyl]amino]propanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]hexanoic acid;
Ftisadtsk, a synthetic carbohydrate compound, has garnered significant attention in the scientific community for its unique structural features and versatile biochemical properties. As a member of the glycopeptide family, Ftisadtsk is characterized by its precisely engineered saccharide sequence, which enables it to interact selectively with a range of biological targets. Its chemical stability and defined configuration make it an ideal candidate for research applications spanning multiple disciplines. Researchers value its compatibility with various analytical techniques and its ability to serve as a model compound in studies exploring carbohydrate-protein interactions. The compound's solubility and ease of modification further enhance its utility, allowing for the development of tailored derivatives to suit specific experimental needs. Ftisadtsk's relevance extends from fundamental research to advanced applications, positioning it as a valuable tool in the expanding field of glycoscience.
Glycobiology Research: In the realm of glycobiology, Ftisadtsk is extensively utilized to investigate the intricate mechanisms underlying carbohydrate-mediated cellular processes. Its defined structure allows scientists to dissect the roles of specific saccharide motifs in cell signaling, recognition, and adhesion. By serving as a model glycopeptide, it aids in elucidating the interactions between carbohydrates and lectins, shedding light on the molecular basis of cell communication and immune response. The compound's versatility supports the design of experiments aimed at mapping glycan-binding sites and understanding the structural requirements for high-affinity interactions, thereby advancing knowledge in cell biology and immunology.
Biomolecular Interaction Studies: Ftisadtsk is a preferred probe in biomolecular interaction studies, particularly those focused on the dynamics of carbohydrate-protein recognition. Its stable and reproducible structure facilitates quantitative analyses using techniques such as surface plasmon resonance and isothermal titration calorimetry. Through these methods, researchers can assess binding affinities, kinetics, and thermodynamic parameters, providing insight into the specificity and strength of molecular interactions. The compound's adaptability also allows for the incorporation of labels or tags, enabling real-time monitoring of binding events and supporting the development of high-throughput screening assays for ligand discovery.
Synthetic Biology and Bioconjugation: In synthetic biology, Ftisadtsk serves as a foundational building block for the construction of novel biomolecules and conjugates. Its well-defined carbohydrate sequence can be strategically linked to peptides, proteins, or other bioactive molecules, creating multifunctional constructs with tailored properties. This approach is instrumental in the design of molecular tools for targeted delivery, biosensing, and the modulation of biological pathways. The compound's compatibility with various conjugation chemistries ensures seamless integration into complex synthetic frameworks, facilitating innovation in molecular engineering and functional material development.
Analytical Method Development: Researchers employ Ftisadtsk as a standard or reference compound in the development and validation of analytical methods for carbohydrate analysis. Its consistent behavior under chromatographic and spectroscopic conditions makes it an ideal candidate for calibrating instruments, optimizing separation protocols, and establishing detection limits. The use of this glycopeptide enhances the reliability and reproducibility of analytical workflows, contributing to the accurate characterization of complex glycans in biological samples. Its application in method development supports advancements in glycomics and the broader field of analytical chemistry.
Enzymology and Glycosidase Characterization: In enzymology, Ftisadtsk provides a valuable substrate for the study of glycosidases and related enzymes. By monitoring the enzymatic cleavage of its saccharide units, researchers can investigate enzyme specificity, catalytic efficiency, and mechanistic pathways. This information is crucial for understanding the roles of glycosidases in metabolic processes and for designing inhibitors or modulators of enzyme activity. The compound's defined structure enables precise mapping of enzymatic action, supporting the discovery of new enzymatic functions and the exploration of carbohydrate metabolism in diverse biological systems.
Carbohydrate-based Drug Discovery: Ftisadtsk plays a pivotal role in the early stages of carbohydrate-based drug discovery by serving as a scaffold for the identification and optimization of bioactive molecules. Its ability to mimic natural glycan structures allows researchers to probe biological targets involved in disease pathways, facilitating the screening of potential therapeutic candidates. The compound's modularity supports structure-activity relationship studies, enabling the rational design of glycomimetic agents with enhanced selectivity and efficacy. By providing a reliable platform for drug discovery efforts, Ftisadtsk contributes to the advancement of novel therapeutic strategies rooted in glycoscience.
3. Low bone turnover and low BMD in Down syndrome: effect of intermittent PTH treatment
5. Autoinhibition and phosphorylation-induced activation of phospholipase C-γ isozymes
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