(2S,4S)-H-L-Pro(4-N3)-OH hydrochloride is a stereospecific proline-based azide ADC linker intermediate facilitating selective click chemistry conjugation for targeted payload delivery in antibody-drug conjugates. Keywords: ADC linker, proline derivative, azide linker, bioorthogonal chemistry, drug delivery.
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Capabilities & Facilities
(2S,4S)-H-L-Pro(4-N3)-OH hydrochloride, a proline derivative commonly utilized in biochemical research and drug development, serves as a cornerstone in various applications explored with high perplexity and burstiness.
Peptide Synthesis: Serving as a fundamental component in peptide and peptidomimetic synthesis, (2S,4S)-H-L-Pro(4-N3)-OH hydrochloride's azide group allows for versatile functionalization via click chemistry, facilitating in-depth studies of protein-protein interactions. Researchers harness this compound to craft precise peptide sequences tailored for diverse biochemical assays, unlocking new avenues in peptide-based research.
Protein Labeling: The exceptional azide functionality of (2S,4S)-H-L-Pro(4-N3)-OH hydrochloride plays a crucial role in bioorthogonal chemistry for protein labeling. Incorporating the azide-modified proline into peptides enables scientists to attach fluorescent dyes or other probes through click reactions, enhancing investigations into protein dynamics and interactions within live cellular environments.
Drug Development: With its potential in designing novel drug candidates, (2S,4S)-H-L-Pro(4-N3)-OH hydrochloride, featuring the azide group, opens avenues for creating proline-rich peptidomimetics with enhanced pharmacokinetic properties. Researchers can evaluate the biological activity of these compounds to unveil promising therapeutic agents, heralding advancements in drug discovery and development.
Structural Biology: Enriching studies in structural biology, (2S,4S)-H-L-Pro(4-N3)-OH hydrochloride finds application in NMR and crystallographic research. Incorporation of this proline derivative into peptides aids in structural determination by providing specific labeling sites, facilitating the elucidation of three-dimensional protein structures and complexes. This knowledge is pivotal in deciphering protein function and strategizing targeted interventions for therapeutic purposes.
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