Fmoc-AEEA-AEEA is a bifunctional linker composed of two aminoethoxyethoxyacetic acid units protected with Fmoc. The flexible spacer supports design of labeled peptides, distance-controlled constructs, and conformational probes. Researchers employ it to tune spacing in biomolecular assemblies. Its hydrophilic nature enhances solubility and synthetic versatility.
CAT No: R2156
CAS No:560088-89-3
Synonyms/Alias:Fmoc-AEEA-AEEA;560088-89-3;Fmoc-o2oc-o2oc-oh;1-(9H-Fluoren-9-yl)-3,12-dioxo-2,7,10,16,19-pentaoxa-4,13-diazahenicosan-21-oic acid;2-[2-[2-[[2-[2-[2-(9H-fluoren-9-ylmethoxycarbonylamino)ethoxy]ethoxy]acetyl]amino]ethoxy]ethoxy]acetic acid;MFCD09752868;Fmoc-8-amino-3,6-dioxaoctanoyl-8-amino-3,6-dioxaoctanoic acid;2-{2-[2-(2-{2-[2-({[(9H-fluoren-9-yl)methoxy]carbonyl}amino)ethoxy]ethoxy}acetamido)ethoxy]ethoxy}acetic acid;Fmoc-AEEA-AEEA-OH;Fmoc-AEEAc-AEEAc-OH;SCHEMBL13942897;ZB0893;AKOS030212490;17-(9-Fluorenylmethyloxycarbonyl-amino)-9-aza-3,6,12,15-tetraoxa-10-on-heptadecanoic acid;FmocNH-PEG2-CH2CONH-PEG2-CH2COOH;AC-32526;BS-17244;FF159078;SY295141;DB-114567;CS-0163267;17-(Fmoc-amino)-10-oxo-3,6,12,15-tetraoxa-9-azaheptadecan-1-oic Acid;1-(9H-Fluoren-9-yl)-3,12-dioxo-2,7,10,16,19-pentaoxa-4,13-diazahenicosan-21-oicacid;[2-(2-{2-[2-(2-{[(9H-fluoren-9-ylmethoxy)carbonyl]amino}ethoxy)ethoxy]acetamido}ethoxy)ethoxy]acetic acid;
Fmoc-AEEA-AEEA is a synthetic peptide building block featuring two units of aminoethoxyethoxyacetic acid (AEEA) linked together and protected at the N-terminus by a fluorenylmethyloxycarbonyl (Fmoc) group. As a hydrophilic, flexible spacer, this compound is widely valued in peptide chemistry for its ability to introduce defined, ethylene glycol-like linkers within peptide chains or between functional groups. Its unique structure imparts enhanced solubility and conformational flexibility, making it a preferred choice for researchers developing complex peptide conjugates, multifunctional bioconjugates, or surface-modified biomaterials. The presence of the Fmoc group enables straightforward incorporation into solid-phase peptide synthesis (SPPS) protocols, supporting precise, stepwise construction of advanced molecular architectures.
Peptide Synthesis: Utilization of Fmoc-AEEA-AEEA as a hydrophilic spacer is common in the solid-phase synthesis of peptides, particularly when spatial separation between functional domains is required. Its ethylene glycol-based backbone introduces flexibility and reduces steric hindrance, allowing for efficient coupling of bulky or sensitive residues. The Fmoc protection facilitates compatibility with standard Fmoc/tBu SPPS strategies, enabling seamless integration into automated or manual synthesis workflows. Researchers leverage its properties to design peptides with improved solubility, reduced aggregation, and enhanced synthetic yield, especially in the assembly of long or branched peptide sequences.
Bioconjugation: In the development of bioconjugates, AEEA-based linkers serve to distance bioactive peptides or ligands from carrier proteins, fluorophores, or solid supports. The presence of two AEEA units in this compound provides an extended, flexible tether that can mitigate steric clashes and preserve the functional integrity of conjugated moieties. This is particularly valuable in the synthesis of peptide-drug conjugates, affinity tags, or labeled peptides, where spatial orientation and accessibility are critical for biological recognition or analytical detection.
Surface Modification: The hydrophilic nature and conformational adaptability of the AEEA spacer make it suitable for surface functionalization applications. Incorporation of this linker into self-assembled monolayers, nanoparticles, or biosensor interfaces can reduce nonspecific adsorption and improve the presentation of bioactive peptides or recognition elements. By providing a defined distance from the surface, it enhances the accessibility and mobility of immobilized molecules, which is essential for optimizing sensor sensitivity, biomolecular interactions, or cell adhesion studies.
Peptide Cyclization and Stapling: The flexible yet hydrophilic properties of the di-AEEA linker support its use in the design of cyclic or stapled peptides. Introduction of this spacer between specific residues can facilitate macrocyclization, stabilize secondary structures, or modulate conformational dynamics. Such modifications are frequently employed to improve the structural stability, proteolytic resistance, or functional display of synthetic peptides, enabling the exploration of novel peptide-based scaffolds for biochemical research.
Analytical Method Development: Researchers incorporate AEEA-based spacers in the synthesis of peptide standards or analytical probes for mass spectrometry, chromatography, or binding assays. The defined length and hydrophilicity of the di-AEEA unit provide consistent physicochemical properties, aiding in method calibration, retention time adjustment, or enhancement of ionization efficiency. This contributes to more reliable quantitation, identification, and characterization of peptide analytes in complex biological mixtures or quality control workflows.
If you have any peptide synthesis requirement in mind, please do not hesitate to contact us at . We will endeavor to provide highly satisfying products and services.
Creative Peptides is a trusted CDMO partner specializing in high-quality peptide synthesis, conjugation, and manufacturing under strict cGMP compliance. With advanced technology platforms and a team of experienced scientists, we deliver tailored peptide solutions to support drug discovery, clinical development, and cosmetic innovation worldwide.
From custom peptide synthesis to complex peptide-drug conjugates, we provide flexible, end-to-end services designed to accelerate timelines and ensure regulatory excellence. Our commitment to quality, reliability, and innovation has made us a preferred partner across the pharmaceutical, biotechnology, and personal care industries.
Read More