MC-VC-PAB-NH2 TFA incorporates a modular cleavable linker system frequently evaluated in controlled-release and protease-cleavage studies. Val-Cit and PAB components shape enzymatic specificity. Researchers analyze its stability, solubility, and kinetic behavior. Applications include prodrug-linker research, reaction monitoring, and controlled-delivery modeling.
CAT No: R2697
CAS No:1616727-21-9
Synonyms/Alias:MC-VC-PAB-NH2 TFA;1616727-21-9;MC-VC-PAB-NH2 (TFA);EX-A8193E;HY-136132A;DA-55297;CS-0311313;[4-[[(2S)-5-(carbamoylamino)-2-[[(2S)-2-[6-(2,5-dioxopyrrol-1-yl)hexanoylamino]-3-methylbutanoyl]amino]pentanoyl]amino]phenyl]methyl N-(2-aminoethyl)carbamate;2,2,2-trifluoroacetic acid;L-Ornithinamide, N-[6-(2,5-dihydro-2,5-dioxo-1H-pyrrol-1-yl)-1-oxohexyl]-L-valyl-N5-(aminocarbonyl)-N-[4-[[[[(2-aminoethyl)amino]carbonyl]oxy]methyl]phenyl]-, 2,2,2-trifluoroacetate (1:1);
MC-VC-Pab-NH2 tfa is a synthetic peptide-based linker commonly utilized in the development of antibody-drug conjugates (ADCs) and related bioconjugation research. Structurally, it features a maleimidocaproyl (MC) moiety, a valine-citrulline (VC) dipeptide sequence, and a para-aminobenzyl (Pab) spacer, terminated with an amide group and provided as a trifluoroacetate (tfa) salt. The combination of these functional elements enables selective and controlled cleavage under specific intracellular conditions, making the linker a valuable tool for site-specific conjugation and targeted payload release. Its modular design and well-characterized cleavage mechanism have established it as a critical component in the field of targeted drug delivery and advanced biochemical engineering.
Antibody-Drug Conjugate Synthesis: MC-VC-Pab-NH2 tfa plays a pivotal role in the construction of site-specific antibody-drug conjugates. The maleimide group allows for stable conjugation to thiol-containing residues on monoclonal antibodies, ensuring robust attachment of cytotoxic or bioactive payloads. The VC dipeptide sequence is recognized and cleaved by cathepsin B and related lysosomal proteases within target cells, enabling precise intracellular release of the conjugated molecule. This selective cleavage is essential for maximizing payload efficacy while minimizing off-target effects, making the linker a preferred choice in ADC research and development.
Bioconjugation Method Development: The modular structure of this peptide linker supports the design and optimization of diverse bioconjugation strategies. Researchers employ MC-VC-Pab-NH2 tfa to evaluate linker stability, cleavage kinetics, and payload release profiles under physiologically relevant conditions. Its well-understood mechanism provides a reliable foundation for comparative studies of linker architectures, facilitating the rational selection and customization of linkers for specific applications in targeted therapeutics, diagnostics, and molecular imaging.
Payload Release Mechanism Studies: In mechanistic investigations, the VC-Pab motif serves as a model system for studying enzyme-triggered release of small molecules from larger biomolecular constructs. The cathepsin-sensitive dipeptide and self-immolative Pab spacer enable systematic analysis of cleavage rates, linker degradation pathways, and payload liberation efficiency. Such studies inform the design of next-generation linkers with improved selectivity and controlled release properties, advancing the broader field of stimuli-responsive bioconjugates.
Targeted Delivery System Engineering: MC-VC-Pab-NH2 tfa is frequently utilized in the engineering of targeted delivery vehicles beyond ADCs, including peptide-drug conjugates, nanoparticle surface modifications, and polymer-drug conjugates. Its incorporation enables researchers to endow delivery systems with protease-sensitive release characteristics, enhancing intracellular targeting and payload activation. The linker's compatibility with a variety of chemical payloads and carrier systems supports innovation in drug delivery platform development and functional material design.
Analytical Method Validation: The well-defined structure and cleavage behavior of MC-VC-Pab-NH2 tfa make it a valuable standard in the validation of analytical methods for bioconjugate characterization. Researchers leverage the linker to develop and refine assays for quantifying conjugation efficiency, monitoring linker stability, and detecting payload release in complex biological matrices. Its predictable fragmentation patterns aid in establishing robust quality control protocols for bioconjugate products, supporting reliable performance in research and development workflows.
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