Biotinyl-Gly-Gly-OH combines a biotin group with a flexible diglycine linker, widely used in affinity-based biochemical systems. The construct offers controllable spacing for protein labeling and immobilization. Its solubility facilitates coupling and detection experiments. Applications include bioassay development, conjugation chemistry, and interaction profiling.
CAT No: R2414
CAS No:120447-60-1
Synonyms/Alias:Biotinyl-Gly-Gly-OH;120447-60-1;2-[[2-[5-(2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl)pentanoylamino]acetyl]amino]acetic acid;FB108309;
Biotinyl-Gly-Gly-OH is a synthetic peptide derivative consisting of a biotin moiety covalently attached to a glycine-glycine dipeptide sequence, terminating with a free carboxyl group. This compound is notable for its dual functionality: the biotin tag enables robust affinity interactions with avidin or streptavidin proteins, while the dipeptide spacer provides flexibility and accessibility for conjugation or further modification. Its well-defined structure makes it a valuable tool in peptide chemistry, molecular biology, and bioconjugation strategies, supporting a wide range of applications that leverage the unique properties of biotin and peptide linkers. Researchers utilize this compound to facilitate detection, purification, and immobilization of biomolecules, as well as to explore structure-function relationships in peptide-based systems.
Affinity Tagging: As a biotinylated dipeptide, this molecule serves as an efficient affinity tag for proteins, peptides, oligonucleotides, or other biomolecules. Its biotin unit binds with high specificity and affinity to avidin or streptavidin-coated surfaces, enabling sensitive detection or selective isolation of tagged entities. The glycine-glycine spacer enhances the spatial presentation of the biotin group, reducing steric hindrance and improving binding efficiency in affinity capture workflows, such as pull-down assays, Western blotting, and immunoprecipitation protocols.
Peptide Synthesis and Labeling: In solid-phase peptide synthesis (SPPS) and related methodologies, Biotinyl-Gly-Gly-OH is frequently utilized as a building block for introducing biotin labels at the N-terminus of custom peptides. The dipeptide spacer ensures that the biotin tag remains accessible after conjugation, preserving its interaction capabilities. This approach is particularly valuable in the design of biotinylated probes, peptide arrays, or functionalized peptides for downstream analytical and preparative applications.
Bioconjugation: The compound's free carboxyl group and biotinylated terminus make it an excellent linker for bioconjugation strategies. Researchers employ it to couple biotin to amine-containing molecules, proteins, or nanoparticles via carbodiimide-mediated chemistry or other coupling techniques. The resulting biotinylated conjugates can be used in a variety of bioanalytical platforms, including surface plasmon resonance, biosensor development, or targeted delivery systems, where precise and stable biotin presentation is required.
Surface Immobilization: Biotinyl-Gly-Gly-OH is widely adopted in surface chemistry for the immobilization of peptides or other ligands onto streptavidin- or avidin-coated substrates. The flexible dipeptide linker ensures optimal orientation and accessibility of the immobilized species, which is critical for applications such as microarray fabrication, biosensor functionalization, and high-throughput screening assays. Its use supports reproducible and high-density surface attachment, facilitating robust and sensitive detection of target analytes.
Protein Interaction Studies: The biotinylated dipeptide is instrumental in studying protein-protein and protein-ligand interactions. By incorporating this tag into peptides or protein fragments, researchers can immobilize interaction partners on streptavidin-coated matrices and systematically analyze binding kinetics, specificity, and affinity. This approach is essential in mapping interaction domains, screening for inhibitors, or characterizing molecular recognition events in a controlled and quantitative manner.
Collectively, these diverse application directions underscore the versatility and technical value of Biotinyl-Gly-Gly-OH in peptide research, bioconjugation, and molecular biology. Its unique combination of a biotin affinity handle and a flexible peptide spacer supports a broad spectrum of experimental designs, enabling precise labeling, efficient immobilization, and reliable capture of biomolecular targets in advanced research workflows.
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