m-PEG17-NHS ester
m-PEG17-NHS ester is a monofunctional polyethylene glycol (PEG) linker featuring an NHS-activated ester for amide-bond formation and a methoxy-terminated PEG chain. The linker consists of a PEG segment of approximately seventeen ethylene glycol units, providing a hydrophilic, flexible spacer that can reduce steric interference and improve solubility of conjugates. In PROTAC and targeted protein degradation workflows, this NHS ester enables covalent coupling to primary amines present on ligands or scaffold components (e.g., lysine residues on peptides/protein tags or amine-functionalized small-molecule handles), thereby generating stable amide linkages. By controlling the effective distance and conformational freedom between the two binding elements of a PROTAC, PEG spacers can help preserve affinity for the E3 ligase and the target protein while facilitating efficient ternary complex formation. This product is therefore valuable for constructing modular degradation systems and for optimizing linker length and physicochemical properties during iterative PROTAC design.
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* For research and manufacturing use only. Not for human or clinical use.
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m-PEG17-NHS ester is a polyethylene glycol (PEG)-based linker designed for efficient conjugation in targeted protein degradation workflows. Its NHS-ester functionality enables robust coupling to primary amines on ligands, facilitating the modular assembly of PROTACs while improving solubility and providing a flexible spacer. The resulting conjugates can better support productive ternary complex formation between target proteins and E3 ligases. Detailed structural and reactivity considerations are provided below.
Structure: The linker comprises a PEG chain terminated with an N-hydroxysuccinimide ester at the para-position relative to the attachment point, providing a flexible, hydrophilic scaffold. It contains an activated carboxylate ester, with stable ether linkages along the PEG backbone and an NHS leaving group.
Reactivity: The NHS ester reacts with primary amines via acyl substitution, forming an amide bond while releasing N-hydroxysuccinimide. Suitable conditions typically use mildly basic aqueous or mixed aqueous/organic buffers to promote nucleophilic attack while minimizing hydrolysis. Common solvents include DMF or DMSO for solubilizing the linker, and the coupling is often performed at controlled temperature with careful timing to limit NHS-ester degradation.
* 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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