H-Lys(biotinyl)-NH2

H-Lys(biotinyl)-NH2 is a lysine-derived amino acid amide/amine building block bearing a biotinylated side chain, where the ε-amino group of L-lysine is functionalized to present a biotin moiety while the α-amino group remains available as a free amino functionality and the α-carboxyl group is present as a terminal amide (NH2). The molecule therefore combines a stereochemically defined L-lysine backbone with two key reactive handles: a primary amine at the α-position for coupling or derivatization, and the biotin functionality that can participate in avidin/streptavidin recognition chemistry. The presence of an unprotected amino group supports peptide coupling strategies and salt formation, while the biotinylated side chain introduces a strong molecular-recognition element that can be carried through downstream conjugation and assay workflows. As a chiral, functionalized amino acid derivative, H-Lys(biotinyl)-NH2 is commonly handled as a research intermediate for constructing biotin-tagged lysine motifs, enabling controlled incorporation of biotin into peptide and biomolecule architectures.

1. Bioconjugation Handles

H-Lys(biotinyl)-NH2 is used in bioconjugation chemistry where the biotinylated lysine side chain enables affinity-based capture and detection using avidin/streptavidin systems. The compound's free α-amino group can be employed for amide bond formation with activated carboxylic acids or for coupling into spacer-bearing conjugates, allowing the biotin tag to be positioned at a defined distance from the attachment point. Biotin recognition can be preserved through appropriate coupling conditions, supporting workflows such as probe generation, pull-down reagents, and affinity standards. Downstream derivatives prepared from this amino acid motif can be incorporated into peptide conjugates, reagent scaffolds, or assay components that rely on robust biotin-protein binding.

2. Peptide Synthesis

H-Lys(biotinyl)-NH2 is applicable to peptide building block preparation and peptide coupling chemistry when lysine residues bearing a biotin handle are required within a peptide sequence or as a terminal functional group. The L-lysine stereocenter and the ε-bioconjugation-ready side chain support incorporation of a biotinylated lysine unit into peptide analogs, while the terminal α-amino functionality can be transformed into a protected or activated form compatible with standard peptide coupling logic. Side-chain biotin can be carried through synthesis provided that protecting-group strategies and coupling chemistries are selected to minimize biotin degradation or unwanted side reactions. Resulting biotin-containing peptides can serve as ligands, imaging probes for biochemical assays, or reference materials for studying peptide-protein interactions.

3. Chemical Biology Probes

H-Lys(biotinyl)-NH2 is suitable for chemical biology research where biotinylated lysine motifs are used to create affinity-tagged probes for target engagement and pathway mapping. The biotin moiety functions as a molecular-recognition element that can enable enrichment of labeled biomolecules after labeling steps, while the amino acid framework supports controlled attachment to other chemical reporters or biomolecular scaffolds. The defined primary amine allows derivatization into amide-linked probes, enabling conjugation to carboxyl-activated dyes, linkers, or functionalized nanoparticles. Biotin-tagged derivatives generated from this compound can be used as biochemical research intermediates for pull-down experiments, proteome fraction enrichment, and analytical capture formats.

4. Protein Engineering Tags

H-Lys(biotinyl)-NH2 is used in protein engineering and biomolecule modification workflows where a lysine-based biotin tag is required for site-specific or motif-based labeling strategies. The compound's chiral lysine backbone can be incorporated into engineered peptide segments or used to generate biotinylated lysine analogs that mimic natural residue spacing in protein-ligand or protein-surface contexts. The biotin functionality supports subsequent affinity capture, while the amino group enables attachment to protein-reactive surfaces through amide formation or linker installation. Downstream products include biotinylated peptide tags, affinity standards for binding assays, and modular labeling reagents used to track biomolecular interactions in applied research settings.

5. Analytical Research Standards

H-Lys(biotinyl)-NH2 is applicable to analytical research and method development where biotin-containing amino acid standards are needed for calibration, enrichment validation, or assay normalization. The biotin moiety provides a strong and selective handle for detection workflows that use streptavidin/avidin reagents, while the amino acid structure supports consistent derivatization into assay-compatible forms. The defined functional groups enable preparation of reference conjugates for LC-MS quantitation, affinity-based enrichment controls, and biotin-binding assay performance checks. Analytical derivatives derived from this compound can serve as reproducible biochemical research intermediates for characterizing labeling efficiency and monitoring conjugation outcomes.

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