mPEG7-thiol is a methoxy-terminated poly(ethylene glycol) chain bearing a terminal thiol, providing a flexible, water-compatible linker suitable for thiol–functionalization chemistries. Structurally, it consists of an mPEG segment with a short PEG chain length and a reactive sulfhydryl group at the terminus, enabling conjugation to maleimide-, iodoacetamide-, or other thiol-reactive handles commonly used in PROTAC and related bifunctional constructs. In targeted protein degradation designs, this linker is used to tune solubility, reduce nonspecific hydrophobic interactions, and spatially separate binding elements so that the recruited E3 ligase and target-binding moieties can engage their respective proteins with improved effective proximity. Its PEG-based, flexible architecture can also facilitate aqueous handling and downstream purification, making it a practical reagent for constructing degraders, molecular glues, and other conjugates that require controlled attachment of functional groups via a terminal thiol.
Structure of 651042-82-9
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mPEG7-thiol is a polyethylene glycol-based thioether/thiol-functional linker designed to support PROTAC assembly and related conjugation strategies by providing a hydrophilic, flexible spacer and a reactive sulfur handle. Its PEG segment can improve solubility and reduce non-specific interactions, while the thiol functionality enables site-selective coupling to electrophilic partners. The product is therefore useful for constructing PROTACs and for preparing linker intermediates that require controlled attachment chemistry; the detailed structural and reactivity features are described below.
Structure: mPEG7-thiol comprises a methoxy-terminated polyethylene glycol chain bearing a terminal thiol group. The structure features an ether-rich PEG backbone with flexible C–O and C–C connectivity, plus a sulfur–hydrogen functional group enabling thiol-mediated conjugation. The PEG segment imparts high polarity and water compatibility.
Reactivity: The terminal thiol can participate in nucleophilic substitution and thiol–electrophile coupling reactions to form stable thioether linkages, commonly via maleimide, haloacetamide, or other activated electrophiles used in bioconjugation workflows. For reliable performance, thiols are typically handled under inert or low-oxidation conditions and in solvents compatible with both thiol stability and the electrophile reactivity. Mild bases or pH-controlled buffers are often used to modulate thiolate formation while minimizing thiol oxidation; reaction progress is generally monitored by chromatographic or spectroscopic methods.
* 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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