Product Name: Ac-EEVC-OH
Sequence: Ac-Glu(t-Bu)-Glu(t-Bu)-Val-citrulline
Purity: 98%
Form: White to off-white Solid
Storage : Sealed storage, away from moisture
CAS.NO.: 2921734-44-1
Chemical Formula: C31H54N6O11
Molar Mass: 686.79
SMILES: CC(C)[C@@H](C(=O)N[C@@H](CCCNC(=O)N)C(=O)O)NC(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)[C@H](CCC(=O)OC(C)(C)C)NC(=O)C
IUPACNAME: (2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-acetamido-5-[(2-methylpropan-2-yl)oxy]-5-oxopentanoyl]amino]-5-[(2-methylpropan-2-yl)oxy]-5-oxopentanoyl]amino]-3-methylbutanoyl]amino]-5-(carbamoylamino)pentanoic acid
INCHIKEY: XYXTYHIOGGKKTC-CIEVZJJWSA-N
INCHI: InChI=1S/C31H54N6O11/c1-17(2)24(27(43)36-21(28(44)45)11-10-16-33-29(32)46)37-26(42)20(13-15-23(40)48-31(7,8)9)35-25(41)19(34-18(3)38)12-14-22(39)47-30(4,5)6/h17,19-21,24H,10-16H2,1-9H3,(H,34,38)(H,35,41)(H,36,43)(H,37,42)(H,44,45)(H3,32,33,46)/t19-,20-,21-,24-/m0/s1
Application: Ac-EEVC-OH is a synthetic peptide-based ADC linker designed for the preparation of antibody-drug conjugate molecules. Its defined amino acid sequence provides a functional linker structure that can support payload attachment, spacing, and conjugation strategy development in targeted drug delivery research. As an ADC linker, Ac-EEVC-OH is useful for constructing experimental conjugates, evaluating linker performance, and studying how linker composition influences stability, release behavior, and overall ADC design. This peptide is widely applied in medicinal chemistry, chemical biology, peptide synthesis, bioconjugation research, and antibody-drug conjugate development for targeted cancer therapy platforms.
Current Research: Ac-EEVC-OH is a peptide-based linker building block used in antibody–drug conjugate, peptide–drug conjugate, and targeted delivery research. The sequence contains glutamic acid, glutamic acid, valine, and cysteine residues with an N-terminal acetyl group and a C-terminal carboxylic acid. This structure gives the molecule several useful features for conjugation chemistry: acidic residues that can improve hydrophilicity and charge balance, a valine residue that can contribute to protease-recognition or spacing behavior depending on the full construct, and a cysteine residue that introduces a thiol-containing side chain suitable for further functionalization. Because linker design is one of the most important determinants of ADC performance, Ac-EEVC-OH is valuable as a modular intermediate for assembling research ADC molecules and related bioconjugates. A major application of Ac-EEVC-OH is ADC linker synthesis. Antibody–drug conjugates are composed of a targeting antibody, a linker, and a payload. The linker must maintain conjugate stability before target-cell delivery while allowing efficient payload release or retention after internalization, depending on the intended design. Ac-EEVC-OH can be incorporated into linker architectures where peptide sequence, hydrophilicity, conjugation site, and release chemistry are systematically optimized. Researchers may use it to build linker-payload intermediates before attachment to antibodies, antibody fragments, nanobodies, proteins, or other targeting platforms. The cysteine residue in Ac-EEVC-OH is particularly important for bioconjugation strategy. Cysteine provides a thiol group that can participate in maleimide coupling, disulfide formation, thiol-ene chemistry, alkylation, or other thiol-selective reactions after appropriate handling. This makes Ac-EEVC-OH useful in workflows where a peptide linker must be connected to a payload, spacer, polymer, resin, fluorescent probe, or targeting molecule through cysteine chemistry. Thiol-based conjugation is widely used because it can provide relatively selective modification under mild conditions. The two glutamic acid residues contribute acidic character and hydrophilicity. In ADC research, hydrophilicity is often critical because many cytotoxic payloads are hydrophobic. Excessive hydrophobicity in linker-payload units can increase aggregation, reduce conjugation efficiency, promote nonspecific binding, and complicate purification. Incorporating acidic residues into a linker can improve aqueous compatibility and help balance hydrophobic payloads or aromatic spacer units. Ac-EEVC-OH may therefore be useful in linker designs intended to improve solubility and reduce nonspecific interactions. Ac-EEVC-OH also supports peptide–drug conjugate research beyond classical antibody conjugates. Peptide–drug conjugates often use a targeting peptide, cleavable or non-cleavable linker, and payload. In these systems, the linker controls distance, flexibility, solubility, enzymatic sensitivity, and release behavior. Ac-EEVC-OH can be incorporated into constructs involving receptor-targeting peptides, tumor-homing peptides, cell-penetrating peptides, peptide hormones, integrin-binding ligands, or biomaterial-targeting sequences. Researchers can evaluate how the EEVC segment affects target binding, cellular uptake, intracellular trafficking, payload release, and biological activity. In targeted delivery research, Ac-EEVC-OH can serve as part of a controlled spacer or functional linker between a targeting domain and a payload. Linker structure can influence whether a conjugate binds its receptor efficiently, avoids steric hindrance, resists premature degradation, or releases its payload under desired conditions. Ac-EEVC-OH-derived linkers may be compared with PEG linkers, polysarcosine linkers, glycine-serine spacers, alkyl linkers, disulfide linkers, Val-Cit systems, GGFG-PAB systems, or other peptide-based linker motifs. The molecule may also be useful in redox-responsive linker research if the cysteine thiol is used to form disulfide-containing conjugates. Disulfide linkers are studied because they may remain relatively stable extracellularly while being cleaved or reduced in intracellular environments with higher reducing potential. Ac-EEVC-OH can provide a cysteine-containing intermediate for building and testing such redox-sensitive systems. In these workflows, researchers evaluate disulfide stability, reduction-triggered payload release, serum stability, intracellular cleavage, and conjugate activity. In protease- or enzyme-responsive linker studies, Ac-EEVC-OH may be incorporated into larger peptide sequences to evaluate whether neighboring residues influence cleavage behavior. Although the isolated EEVC sequence should not automatically be assumed to have a specific protease selectivity, it can contribute to broader linker architecture in enzymatically responsive constructs. Cleavage studies may use purified proteases, lysosomal extracts, cell lysates, serum-like matrices, HPLC, LC-MS, and release-product analysis. Ac-EEVC-OH is also relevant to chemical biology probe construction. The peptide may be used to build fluorescent conjugates, affinity probes, biotinylated molecules, immobilized ligands, or peptide-based assay reagents. The acidic residues may improve solubility, while the cysteine residue provides a site for selective attachment of reporter groups or surfaces. Such probes can be used to study binding, uptake, release, and stability of linker-containing constructs. Analytical characterization is important when using Ac-EEVC-OH in ADC synthesis. Researchers typically confirm identity and purity by HPLC and LC-MS, monitor cysteine oxidation state, evaluate solubility, and confirm coupling efficiency during multistep synthesis. Since cysteine can oxidize to disulfides, storage and reaction conditions should be controlled carefully. Reducing agents, oxygen exposure, pH, buffer composition, and metal contamination can affect thiol reactivity. Recommended controls include linker-free conjugates, cysteine-free analogs, non-cleavable linker comparators, hydrophilic linker controls, payload-only controls, antibody-only controls, thiol-blocked controls, serum stability assays, reducing-condition release assays, and LC-MS confirmation of conjugation products. For ADC workflows, additional characterization should include drug-to-antibody ratio, aggregation analysis by SEC-HPLC, hydrophobic interaction chromatography, free payload detection, conjugation site analysis, and stability testing. Overall, Ac-EEVC-OH is a useful peptide-based ADC linker building block for bioconjugation and targeted delivery research. It supports antibody–drug conjugate synthesis, peptide–drug conjugate construction, cysteine-mediated coupling, hydrophilic linker optimization, redox-responsive design, chemical biology probe development, payload attachment chemistry, and systematic evaluation of linker structure in next-generation ADC and biomolecular delivery platforms.
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