Mal-PEG8-OH
Mal-PEG8-OH is a mono-functional maleimide-terminated polyethylene glycol linker featuring a single hydroxyl group at one terminus and an eight-unit PEG chain that provides a flexible, hydrophilic spacer. The maleimide moiety is designed for chemoselective conjugation to thiols via Michael addition, enabling stable thioether bond formation under mild aqueous conditions. In PROTAC architectures, this type of linker is valuable for connecting a thiol-bearing ligand (for example, a cysteine-functionalized binding handle on an E3 ligase recruiter or target-binding moiety) to the complementary component while minimizing steric hindrance and preserving binding affinity. The PEG segment improves solubility and can reduce non-specific interactions, often facilitating more reproducible synthesis and purification of conjugates. Researchers use Mal-PEG8-OH to systematically tune linker length and polarity in targeted protein degradation studies, supporting the development and optimization of degraders with improved cellular performance and experimental tractability.
Structure of 2353409-63-7
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* For research and manufacturing use only. Not for human or clinical use.
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Mal-PEG8-OH is a maleimide-terminated polyethylene glycol linker designed for robust, site-selective conjugation in targeted protein degradation workflows. Its maleimide handle enables efficient coupling to thiol-bearing ligands, while the PEG spacer improves aqueous solubility and helps modulate linker flexibility and overall PROTAC architecture. The resulting conjugates are commonly used to assemble bifunctional degraders that recruit an E3 ligase and a target protein; detailed structural and reactivity considerations are provided below.
Structure: Mal-PEG8-OH is composed of a maleimide moiety linked to a polyethylene glycol chain terminating in a hydroxyl group. It contains a cyclic imide with an activated alkene suitable for Michael-type addition, along with ether linkages that confer hydrophilicity and conformational flexibility.
Reactivity: The maleimide group reacts with free thiols via a Michael addition under mild aqueous conditions, forming a stable thioether linkage. Suitable ligands bearing cysteine, reduced disulfides, or other thiol functionalities can be coupled without harsh reagents. Reaction performance is typically optimized by maintaining near-neutral pH, using thiol-compatible buffers, and avoiding strong competing nucleophiles or oxidizing conditions that would consume reactive thiols.
* 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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