Mal-amido-PEG2-Val-Cit-PAB-PNP integrates a PEG spacer, cleavable linker, and chromogenic group that support reaction monitoring. The Val-Cit motif provides enzyme-responsive behavior useful for studying cleavage kinetics. Researchers analyze its stability, solubility, and linker reactivity. Applications include targeted-delivery models, protease characterization, and synthetic conjugation studies.
CAT No: R2643
CAS No:2112738-13-1
Synonyms/Alias:Mal-amido-PEG2-Val-Cit-PAB-PNP;2112738-13-1;[4-[[(2S)-5-(carbamoylamino)-2-[[(2S)-2-[3-[2-[2-[3-(2,5-dioxopyrrol-1-yl)propanoylamino]ethoxy]ethoxy]propanoylamino]-3-methylbutanoyl]amino]pentanoyl]amino]phenyl]methyl (4-nitrophenyl) carbonate;MFCD30828687;{4-[(2S)-5-(carbamoylamino)-2-[(2S)-2-[3-(2-{2-[3-(2,5-dioxo-2,5-dihydro-1H-pyrrol-1-yl)propanamido]ethoxy}ethoxy)propanamido]-3-methylbutanamido]pentanamido]phenyl}methyl 4-nitrophenyl carbonate;EX-A5857;AKOS040742063;BP-23675;DA-55189;HY-140147;CS-0115252;C70532;
Mal-amido-PEG2-Val-Cit-PAB-PNP is a heterobifunctional chemical linker belonging to the class of peptide-based conjugation reagents, specifically designed for advanced bioconjugation and drug development research. Structurally, it features a maleimide group for selective thiol reactivity, a polyethylene glycol (PEG2) spacer to enhance solubility and reduce steric hindrance, and a valine-citrulline (Val-Cit) dipeptide motif connected to a para-aminobenzyl (PAB) self-immolative spacer, terminating in a p-nitrophenyl (PNP) carbonate. This modular architecture enables site-specific conjugation, controlled payload release, and improved pharmacokinetic profiles, making the compound highly relevant for the construction of antibody-drug conjugates (ADCs) and other targeted delivery systems in biochemical research.
Antibody-drug conjugate (ADC) development: As a cleavable peptide-based linker, Mal-amido-PEG2-Val-Cit-PAB-PNP is widely utilized in the synthesis of ADCs. The Val-Cit dipeptide sequence is specifically recognized and cleaved by cathepsin B and related lysosomal proteases, facilitating the controlled intracellular release of cytotoxic payloads upon internalization by target cells. The maleimide moiety enables site-specific attachment to cysteine residues on antibodies, while the PAB self-immolative spacer ensures efficient drug liberation following enzymatic cleavage. This mechanism is critical for achieving selective cytotoxicity and minimizing off-target effects during preclinical ADC evaluation.
Targeted bioconjugation studies: The heterobifunctional nature of the linker allows for the precise attachment of diverse biomolecules, such as peptides, proteins, or small-molecule drugs, to carrier systems. The maleimide group reacts efficiently with thiol-containing ligands, and the PNP carbonate provides an orthogonal handle for coupling with amines. This dual reactivity supports the construction of multifunctional conjugates, facilitating mechanistic studies of targeted delivery, receptor-mediated uptake, and intracellular trafficking in a variety of experimental models.
Enzyme-responsive linker research: The Val-Cit-PAB motif serves as a model for enzyme-cleavable linkers, enabling researchers to investigate the kinetics and specificity of protease-mediated release mechanisms. Studies employing this linker can elucidate the role of cathepsin B and related enzymes in payload liberation, supporting the rational design of next-generation cleavable linkers for improved selectivity and efficacy in targeted delivery applications.
Payload release mechanism analysis: The self-immolative PAB spacer incorporated within the linker architecture allows for detailed examination of payload release kinetics following enzymatic cleavage. By monitoring the breakdown of the linker and subsequent drug liberation, researchers can optimize conjugate design for maximal payload stability in circulation and rapid, complete release in target environments. This application is essential for fine-tuning the balance between systemic stability and efficient intracellular delivery in bioconjugate research.
Synthetic chemistry and linker optimization: Chemists and formulation scientists leverage the modular structure of Mal-amido-PEG2-Val-Cit-PAB-PNP to develop and optimize new linker systems with tailored properties. The PEG2 spacer can be varied to adjust hydrophilicity and steric accessibility, while modifications to the peptide sequence or terminal groups enable the exploration of structure-activity relationships. Such studies contribute to the advancement of linker technology for use in a broad spectrum of targeted delivery platforms and molecular probes.
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