Mal-PEG12-Boc
Mal-PEG12-Boc is a heterobifunctional polyethylene glycol (PEG) linker featuring a maleimide group for selective thiol conjugation and a Boc-protected functionality that can be used to tune reactivity and synthetic handling. Structurally, it comprises a PEG chain of moderate length that provides aqueous solubility, conformational flexibility, and reduced nonspecific interactions, while the maleimide enables rapid, chemoselective coupling to cysteine-containing ligands or engineered proteins via Michael addition to form stable thioether linkages. In PROTAC and targeted protein degradation workflows, such linkers are commonly employed to connect an E3-ligase-recruiting moiety to a targeting ligand or to incorporate a spacer that optimizes geometry, improves effective molarity, and can modulate degradation potency by influencing linker length and hydrophilicity. Its PEG-based architecture makes it a useful tool for systematic linker optimization and for generating well-defined conjugates for biochemical and cellular degradation assays.
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* For research and manufacturing use only. Not for human or clinical use.
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Mal-PEG12-Boc is a bifunctional PEG-based PROTAC linker building block designed to combine a maleimide electrophile with a tert-butyl ester-protected carboxyl handle. Its flexible polyethylene glycol segment improves solubility and linker dynamics, while the maleimide enables selective conjugation to thiol-containing ligands. This combination supports efficient assembly of targeted protein degraders, and the subsequent points describe its structure and practical reactivity considerations in detail.
Structure: The linker comprises a maleimide group for Michael-type thiol addition, a PEG chain providing conformational flexibility, and a tert-butyl ester-protected carboxyl group for orthogonal functionalization. It contains conjugated alkene functionality in the maleimide ring, ether linkages within the PEG backbone, and ester chemistry associated with tert-butyl carboxyl protection.
Reactivity: Maleimide participates in thiol–maleimide conjugation under aqueous or mixed aqueous conditions, typically using mild bases to maintain thiolate availability while minimizing maleimide hydrolysis. The reaction proceeds via a Michael addition to form a stable thioether linkage, commonly without metal catalysts. The tert-butyl ester can be cleaved under standard acid-mediated conditions to reveal the carboxylic acid for subsequent activation and coupling steps.
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
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