(R)-8-Azido-2-(Fmoc-amino)octanoic acid is a non-cleavable ADC linker used in the synthesis of antibody-drug conjugates (ADCs).
Structure of 1191429-18-1
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(R)-8-Azido-2-(Fmoc-amino)octanoic acid, a specialized chemical compound used in peptide synthesis and bioorthogonal chemistry, finds diverse applications in the scientific realm. Here are four key applications presented with a high degree of perplexity and burstiness:
Peptide Synthesis: Employing (R)-8-Azido-2-(Fmoc-amino)octanoic acid in peptide synthesis allows for the incorporation of azide groups into peptide chains, enabling subsequent conjugation reactions like "click chemistry" to attach diverse functional groups or labels onto peptides. This process is instrumental in crafting bespoke peptides tailored for both research endeavors and therapeutic interventions.
Bioorthogonal Chemistry: The reactive nature of the azide group in (R)-8-Azido-2-(Fmoc-amino)octanoic acid makes it a key player in bioorthogonal reactions that seamlessly operate alongside natural biological processes. Widely utilized for labeling and tracking biomolecules in live cells, this compound facilitates precise exploration of biomolecular interactions and dynamics within their native cellular milieu, offering invaluable insights into the intricacies of biological systems.
Drug Development: In the realm of drug development, (R)-8-Azido-2-(Fmoc-amino)octanoic acid plays a pivotal role in creating novel drugs and bioconjugates. By integrating this compound into drug molecules, researchers can explore innovative drug delivery systems and targeted therapeutic approaches, potentially enhancing drug efficacy while minimizing undesirable side effects, thus revolutionizing the landscape of pharmaceutical interventions.
Proteomics: Within the domain of proteomic studies, (R)-8-Azido-2-(Fmoc-amino)octanoic acid serves as a valuable tool for tagging and identifying proteins. Leveraging the azide group for attaching tags facilitates the isolation and analysis of specific proteins from complex biological samples, shedding light on protein functions and interactions within diverse biological contexts, thereby advancing our understanding of the intricacies of proteomic landscapes.
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