MC-VC-PAB-NH2 incorporates a maleimide-capable moiety, a Val-Cit protease-cleavable linker, and a para-aminobenzyl self-immolative spacer. The construct is frequently evaluated as a modular unit in conjugate and prodrug design. Researchers quantify cleavage kinetics and payload-release profiles in enzymatic systems. Applications include linker-technology optimization, targeted-delivery modeling, and protease-mechanism studies.
CAT No: R2710
CAS No:1616727-20-8
Synonyms/Alias:MC-VC-PAB-NH2;1616727-20-8;SCHEMBL15868007;{4-[(2S)-5-(carbamoylamino)-2-[(2S)-2-[6-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)hexanamido]-3-methylbutanamido]pentanamido]phenyl}methyl N-(2-aminoethyl)carbamate;AKOS040756930;[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;DA-55296;HY-136132;CS-0119676;
MC-VC-Pab-NH2 is a synthetic peptide-linker conjugate widely utilized in the field of bioconjugation and targeted drug delivery research. Structurally, it consists of a maleimidocaproyl (MC) group, a valine-citrulline (VC) dipeptide sequence, and a para-aminobenzyl (Pab) spacer, terminating in an amide group. This modular design is especially significant for its role as a cleavable linker, enabling controlled release mechanisms in conjugated biomolecules. The MC-VC-Pab-NH2 construct is of particular interest for applications involving antibody-drug conjugates (ADCs) and related targeted delivery systems, owing to its enzymatically cleavable properties and established compatibility with thiol-reactive payloads.
Antibody-Drug Conjugate Research: In the development of ADCs, MC-VC-Pab-NH2 serves as a critical linker moiety that connects cytotoxic agents to monoclonal antibodies. Its VC peptide sequence is selectively cleaved by lysosomal proteases, such as cathepsin B, within targeted cells, allowing for the intracellular release of the drug payload. This feature makes the linker highly valuable for researchers designing next-generation ADCs with improved selectivity and reduced systemic toxicity, enabling precise evaluation of linker-dependent pharmacokinetics, stability, and release profiles in preclinical models.
Bioconjugation Method Development: The maleimide functionality present in MC-VC-Pab-NH2 facilitates site-specific conjugation to thiol-containing biomolecules, such as cysteine residues on proteins or peptides. This enables the construction of homogeneous conjugates with controlled stoichiometry, an essential factor in the reproducibility and efficacy of bioconjugate products. Researchers employ this linker to optimize conjugation protocols, assess linker-payload stability, and refine techniques for the assembly of multifunctional biotherapeutics or diagnostic agents.
Enzyme-Responsive Delivery Systems: The protease-cleavable VC-Pab motif within the linker is extensively studied for its application in enzyme-responsive delivery platforms. By exploiting the differential expression of lysosomal proteases in various cell types, scientists can design delivery vehicles that release their active cargo preferentially within targeted intracellular environments. This approach supports the development of advanced delivery systems for small molecules, peptides, or imaging agents, providing a robust tool for investigating intracellular trafficking and release mechanisms.
Peptide Synthesis and Linker Optimization: MC-VC-Pab-NH2 is frequently used as a model system in peptide synthesis and linker optimization studies. Its modular architecture allows for systematic investigation of how linker structure influences cleavage kinetics, stability under physiological conditions, and compatibility with diverse payloads. Synthetic chemists and formulation scientists utilize this compound to evaluate new linker designs, improve synthetic strategies, and benchmark linker performance in a range of biochemical assays.
Analytical Method Validation: The defined structure and predictable cleavage behavior of MC-VC-Pab-NH2 make it a valuable reference compound for validating analytical methodologies. Techniques such as mass spectrometry, HPLC, and enzyme kinetics assays benefit from the use of this linker in establishing detection parameters, quantifying cleavage products, and calibrating assay sensitivity. By providing a consistent and well-characterized standard, it supports robust analytical workflows essential for quality control and research reproducibility in bioconjugate development.
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