m-PEG36-Mal
m-PEG36-Mal is a methoxy-terminated PEG linker bearing a terminal maleimide group, designed for stable, site-selective conjugation in targeted protein degradation workflows. Structurally, it consists of a long ethylene glycol oligomer chain that provides aqueous solubility and conformational flexibility, terminating in a maleimide electrophile suitable for rapid Michael-type addition with thiols. In PROTAC construction, this linker can be used to connect a thiol-bearing ligand or recruiter module to another component, while the PEG spacer helps reduce steric hindrance and can improve effective molarity at the ternary-complex interface. The maleimide functionality enables controlled attachment to cysteine-containing proteins, peptides, or engineered ligands, facilitating modular synthesis and subsequent purification. Overall, m-PEG36-Mal is valuable for researchers seeking robust PEG-based spacing and efficient thiol–maleimide coupling to optimize linker length and geometry in targeted degradation experiments.
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* For research and manufacturing use only. Not for human or clinical use.
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This m-PEG36-Mal linker is a polyethylene glycol-based maleimide functional linker designed for efficient conjugation in PROTAC workflows. Its flexible PEG scaffold helps tune solubility and presentation of the reactive handle, while the maleimide moiety enables selective coupling to appropriate thiol-containing partners. These features make it suitable for constructing targeted protein degraders where stable, well-defined linker chemistry supports reliable assembly; detailed structural and reactivity considerations are provided below.
Structure: The linker consists of a methoxy-capped PEG chain bearing a terminal maleimide group. It features ether linkages along the PEG backbone and a cyclic imide (maleimide) electrophile. The PEG segment imparts hydrophilicity and conformational flexibility, supporting aqueous compatibility and controlled conjugation behavior.
Reactivity: Maleimide groups typically undergo thiol–maleimide addition under mildly basic conditions, proceeding via nucleophilic attack of a thiolate on the activated alkene within the maleimide ring. Conjugation is commonly performed in aqueous or mixed aqueous buffers using thiol-bearing ligands or intermediates. Reaction rates depend on pH and thiol availability; freshly generated thiols and appropriate buffer choice are often used to minimize side reactions such as hydrolysis or disulfide exchange.
* 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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