Bis-Mal-PEG7
Bis-Mal-PEG7 is a homobifunctional polyethylene glycol (PEG) linker bearing two maleimide groups, enabling efficient thiol–maleimide conjugation to cysteine-containing ligands or engineered proteins. Structurally, it provides a flexible, hydrated PEG chain of intermediate length that spatially separates the two reactive termini, helping reduce steric hindrance and preserve binding of each PROTAC-relevant module. In targeted protein degradation designs, Bis-Mal-PEG7 is used to connect two components—such as a ligand for an E3 ligase and a ligand for the target protein—by forming stable thioether linkages with thiols introduced on the respective building blocks. This linker architecture supports controlled geometry and tunable effective molarity, which can improve formation of the ternary complex and thereby enhance degradation efficiency. Its PEG-based, dual-reactive format is valuable for rapid PROTAC assembly and for systematic linker optimization in degradation research.
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* For research and manufacturing use only. Not for human or clinical use.
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Bis-Mal-PEG7 is a bifunctional, maleimide-terminated polyethylene glycol linker designed to enable efficient conjugation in PROTAC workflows. Its dual reactive termini support modular assembly of targeted protein degraders by linking a ligand-bearing cysteine handle to a second functional partner under mild, aqueous-compatible conditions. The flexible PEG scaffold can help tune solubility and reduce steric constraints, supporting robust synthesis and subsequent biological evaluation. Detailed structural and reactivity considerations are provided below.
Structure: Bis-Mal-PEG7 contains a central polyethylene glycol chain flanked by two maleimide groups. The maleimide rings provide electrophilic alkene functionality for selective thio-Michael addition, while the ether-rich PEG segment confers flexibility, hydrated character, and improved solubility. The linker is typically stable under non-nucleophilic conditions.
Reactivity: PROTAC construction using this linker commonly relies on thio-Michael conjugation between maleimides and thiol-containing partners (e.g., cysteine residues or thiol-functionalized ligands). Reactions are generally performed in aqueous or mixed aqueous buffers at near-neutral pH to preserve maleimide reactivity while minimizing side reactions such as hydrolysis. Thiol activation and careful control of stoichiometry and order of addition help drive selective bis-conjugation without overreaction.
* 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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