DSPE-PEG36-mal
Cat No.: BP-502103
4.5 
DSPE-PEG36-mal is an amphiphilic PEG-based linker built from DSPE (a phospholipid anchor) connected to a long polyethylene glycol chain terminated with a maleimide group. The PEG segment provides a hydrophilic, flexible spacer that helps reduce steric constraints and improves solubility and colloidal stability, while the DSPE moiety enables membrane or lipid-phase association, allowing the conjugate to localize near lipid bilayers or lipid-displayed targets. The terminal maleimide is a thiol-reactive handle that forms stable thioether bonds with cysteine-containing ligands, enabling efficient conjugation to thiol-functionalized binding domains, peptides, or other PROTAC components. In targeted protein degradation research, this linker can be used to construct modular, lipid-associated or membrane-proximal degradation systems, facilitating controlled assembly of multicomponent degraders and supporting studies of how spatial presentation influences ubiquitin–proteasome engagement and ternary complex formation.
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* For research and manufacturing use only. Not for human or clinical use.
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DSPE-PEG36-mal is a PEG-based, lipid-anchored linker designed for constructing PROTACs and related targeted protein degradation conjugates. Its amphiphilic architecture supports stable conjugate formation and facilitates efficient presentation of reactive handles for coupling to ligands. The PEG spacer helps modulate solubility and accessibility, which can improve effective engagement between the target-binding and E3-recruiting components. Detailed structural and reactivity considerations are provided below to guide experimental design.
Structure: The molecule combines a phospholipid (DSPE) hydrophobic anchor with a long polyethylene glycol chain terminated by a maleimide group. It contains ester and ether linkages within the PEG segment and a maleimide electrophile capable of selective addition. Overall, it is amphiphilic and typically forms well-dispersed conjugates in aqueous media.
Reactivity: The terminal maleimide undergoes thiol–maleimide Michael-type addition under mild conditions, enabling conjugation to cysteine-containing ligands or thiol-functionalized partners. Reactions are commonly performed in aqueous or mixed aqueous buffers at near-neutral pH to preserve maleimide reactivity while minimizing side reactions. Mild bases or buffering systems can be used to maintain thiol availability; catalysts are generally not required. Solvents that maintain solubility without destabilizing the maleimide are preferred.
* 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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