Fmoc-NH-PEG1-NHS ester
CAS No.: 1807521-05-6
Cat No.: BP-500603
Purity: ≥95%
4.5 
Fmoc-NH-PEG1-NHS ester is an activated, heterobifunctional PEG-based linker designed for amide-bond formation in PROTAC and targeted protein degradation workflows. Structurally, it combines an Fmoc-protected amine on one end with a N-hydroxysuccinimide (NHS) ester on the other, separated by a short, one-unit polyethylene glycol (PEG) spacer that provides modest hydrophilicity and conformational flexibility. In PROTAC construction, the NHS ester reacts with primary amines present on ligands or linker-bearing intermediates to form stable amide conjugates, while the Fmoc group enables controlled stepwise synthesis and purification during assembly. This linker is particularly useful for generating well-defined conjugation handles that preserve the functional presentation of targeting moieties and recruited-protein ligands, thereby supporting systematic structure–activity studies. Its PEG spacing can help reduce steric clashes and improve coupling efficiency, facilitating reproducible synthesis of degradation candidates for in vitro evaluation.
Structure of 1807521-05-6
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Fmoc-NH-PEG1-NHS ester is a PEG-based bifunctional linker designed for efficient conjugation in PROTAC assembly workflows. It combines an Fmoc-protected amine handle with an NHS-activated ester for rapid coupling to primary amines on targeting ligands or other PROTAC components. The PEG segment improves solubility and can help modulate linker flexibility, supporting productive ternary complex formation. The detailed structural and reactivity characteristics are described below.
Structure: The molecule contains an Fmoc-protected nitrogen attached to a short polyethylene glycol spacer and an NHS-activated carboxylate ester. It features aromatic carbamate functionality, ether linkages within the PEG chain, and an activated N-hydroxysuccinimide ester that is susceptible to nucleophilic acyl substitution.
Reactivity: The NHS ester typically reacts with primary amines under mild, aqueous-compatible conditions to form stable amide bonds. Suitable bases and buffering systems are selected to maintain amine nucleophilicity while minimizing hydrolysis of the activated ester. Common coupling approaches use polar aprotic or buffered aqueous solvents, with temperature kept moderate to preserve reactivity. The process proceeds via nucleophilic acyl substitution, and the Fmoc group can be removed when an exposed amine is required for subsequent coupling steps.
* 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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