Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar

Product Name: Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar

Sequence: Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar

Purity: 99% Form: White to light yellow Solid-Liquid Mixture

Storage : Sealed storage, away from moisture

CAS.NO.: 2857963-60-9

Chemical Formula: C32H54N10O12

Molar Mass: 770.83

SMILES: CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)N(C)CC(=O)O

IUPACNAME: 2-[[2-[[2-[[2-[[2-[[2-[[2-[[2-[[2-[[2-[acetyl(methyl)amino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetyl]-methylamino]acetic acid

INCHIKEY: VBFSXYRMXNNFQG-UHFFFAOYSA-N

INCHI: InChI=1S/C32H54N10O12/c1-22(43)33(2)12-23(44)34(3)13-24(45)35(4)14-25(46)36(5)15-26(47)37(6)16-27(48)38(7)17-28(49)39(8)18-29(50)40(9)19-30(51)41(10)20-31(52)42(11)21-32(53)54/h12-21H2,1-11H3,(H,53,54)

Application: Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is a synthetic decapeptide composed of an acetylated N-methyl glycine residue followed by a polysarcosine chain. Its sarcosine-rich structure provides a hydrophilic, flexible, and biocompatible linker segment suitable for bioconjugation design. This peptide can be used in the preparation of antibody-drug conjugates, where linker properties influence solubility, spacing, payload attachment, and overall conjugate performance. Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is valuable for ADC linker research, peptide synthesis, drug delivery studies, and development of advanced conjugation strategies for targeted therapeutic platforms.

Current Research: Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is a defined decapeptide built from N-methylglycine-derived units, including sarcosine residues, and designed for use in linker and bioconjugation research. Sarcosine, also known as N-methylglycine, is a small N-methylated amino acid that forms hydrophilic, flexible, and peptoid-like oligomeric structures when incorporated repeatedly. Because of this architecture, Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is useful as a structurally controlled spacer in antibody–drug conjugates, peptide–drug conjugates, targeted delivery constructs, and functional biomolecule modification workflows. A major application of this decapeptide is antibody–drug conjugate preparation. ADCs require linkers that connect a targeting antibody to a payload while preserving stability, solubility, conjugation efficiency, and biological function. The linker region strongly affects drug-to-antibody ratio, aggregation tendency, payload exposure, plasma-like stability, internalization behavior, and release profile. A sarcosine-rich decapeptide can serve as a hydrophilic spacer to reduce steric interference between antibody and payload and improve handling of complex linker-payload intermediates. Sarcosine-based linkers are especially useful because they provide an alternative to conventional PEG spacers. PEG linkers are widely used to increase solubility and flexibility, but researchers increasingly evaluate polysarcosine and oligosarcosine motifs because they offer peptide-like synthetic compatibility, defined chain length, hydrophilicity, and low nonspecific interaction potential. Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar provides a discrete decapeptide-length linker rather than a broad-distribution polymer, improving reproducibility in synthetic and analytical workflows. In ADC linker design, hydrophilicity is a major concern. Many cytotoxic payloads are hydrophobic, and hydrophobic linker-payload structures can increase aggregation, reduce conjugate stability, impair pharmacological behavior, and complicate purification. Incorporation of an oligosarcosine decapeptide can help balance hydrophobic payload components by improving aqueous compatibility and reducing nonspecific self-association. This is particularly important in ADCs carrying highly potent hydrophobic drugs, dual-drug linkers, imaging payloads, or bulky aromatic structures. Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is also valuable in peptide–drug conjugate research. Peptide–drug conjugates often combine a targeting peptide, linker, and payload. The linker must provide enough distance for receptor recognition while maintaining solubility and minimizing nonspecific uptake. A sarcosine-rich decapeptide spacer can improve presentation of targeting motifs such as RGD peptides, GLP-1 analogs, tumor-homing peptides, receptor ligands, or cell-penetrating peptide systems. Researchers may compare constructs with and without the sarcosine spacer to evaluate effects on receptor binding, cell uptake, payload delivery, and biological activity. The N-methylated backbone gives this molecule additional research value. N-methylation reduces backbone hydrogen-bond donation and can alter protease susceptibility, conformational flexibility, and solvation behavior. Oligosarcosine linkers may therefore show improved stability relative to some conventional peptide spacers while retaining compatibility with peptide synthesis and bioconjugation chemistry. These properties make the decapeptide useful for linker optimization in biologically complex environments. In targeted delivery research, the compound can support construction of multifunctional conjugates. It may be used as a spacer between a targeting ligand and a payload, between a protein and an imaging probe, or between a nanoparticle surface and a receptor-binding peptide. By increasing the distance from the carrier surface, the sarcosine-rich linker can reduce steric shielding and improve accessibility of the functional domain. This is relevant to nanoparticle functionalization, liposome targeting, polymer conjugates, micelles, peptide-coated surfaces, and affinity probes. The decapeptide can also support chemical biology probe development. Hydrophilic sarcosine spacers are useful in fluorescent probes, biotinylated ligands, photoaffinity reagents, enzyme substrates, receptor ligands, and pull-down tools. In these systems, the linker helps separate the detection tag or affinity handle from the bioactive recognition element. This can improve signal quality, reduce nonspecific binding, and preserve target engagement. In synthetic workflows, Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar may be used as a defined intermediate for building more complex linker-payload units. Researchers can attach cleavable motifs, self-immolative spacers, maleimide handles, azide or alkyne groups, payloads, fluorophores, or targeting ligands depending on the available terminal chemistry and protecting group strategy. Analytical characterization typically includes HPLC purity analysis, LC-MS identity confirmation, solubility assessment, and stability testing. This compound is also useful in comparative linker studies. Researchers can compare oligosarcosine decapeptide linkers with PEG linkers, alkyl linkers, glycine-serine linkers, aminohexanoic acid spacers, polysarcosine chains of different lengths, and charged amino acid linkers. Key performance parameters include solubility, conjugation yield, aggregation, receptor binding, enzymatic stability, serum stability, cell uptake, payload release, and nonspecific adsorption. Recommended controls include linker-free conjugates, PEG-linked analogs, shorter and longer sarcosine oligomers, payload-only controls, targeting ligand-only controls, non-targeted conjugates, and vehicle controls. For ADC-related research, additional characterization should include conjugation efficiency, drug-to-antibody ratio, SEC-HPLC aggregation analysis, hydrophobic interaction chromatography, stability in serum-like media, and payload release profiling. Overall, Ac-{Gly(N-me)}-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar-Sar is a valuable oligosarcosine decapeptide linker for ADC and bioconjugation research. It supports antibody–drug conjugate preparation, peptide–drug conjugate design, hydrophilic spacer optimization, targeted delivery systems, chemical biology probe construction, solubility improvement, linker structure–activity studies, and development of next-generation conjugation strategies requiring a flexible, defined, and water-compatible sarcosine-rich linker.

Reference: Zhang, H., & Meng, X. (2024). U.S. Patent Application No. 18/557,454.