H-Lys(biotinyl)-OH

H-Lys(biotinyl)-OH is a lysine-derived amino acid bearing a biotin moiety attached to the side-chain ε-amino group, retaining the α-amino and α-carboxylic acid functionalities in a free, amino-acid form. The molecule is chiral at the lysine α-carbon and presents a polar, zwitterion-capable backbone alongside a highly functionalized biotin scaffold containing a ureido ring and a valeric acid side chain. The biotinylated side chain introduces multiple hydrogen-bonding sites and a strong affinity handle for streptavidin/avidin recognition, while the terminal carboxylic acid enables coupling or salt formation under standard amino-acid chemistry. Lysine's side-chain attachment point and the biotin's heteroatom-rich framework make the compound suitable as a biochemical labeling intermediate and as a peptide or polymer conjugation precursor where controlled attachment of a targeting/affinity tag is required.

1. Bioconjugation Labeling

H-Lys(biotinyl)-OH is used in chemical biology and bioconjugation workflows where a defined biotin affinity motif is required on an amino-acid scaffold. The lysine backbone provides an α-amino/α-carboxyl handle for subsequent peptide coupling, while the biotinylated ε-amino substituent presents the streptavidin-binding epitope for affinity capture and detection. The presence of multiple heteroatoms in the biotin ring supports stable conjugate formation and can be leveraged for constructing affinity-tagged probes without altering the underlying lysine stereochemistry. Downstream, the compound can serve as a building block for biotinylated reagents, affinity purification standards, and labeling intermediates used in biomolecule modification and assay development.

2. Peptide Synthesis Incorporation

H-Lys(biotinyl)-OH is suitable for peptide building block preparation and for constructing affinity-bearing peptide conjugates via standard amino-acid coupling chemistry. The free α-amino and α-carboxyl groups enable incorporation as a lysine-derived residue, while the biotinylated side chain behaves as a bulky, functional substituent that can be introduced at a defined position in a peptide sequence. Protecting-group strategies commonly applied to lysine derivatives, such as temporary masking of the α-amino and α-carboxyl during assembly, can be used to maintain compatibility with peptide coupling reagents while preserving the biotin functionality for later binding. The resulting biotin-containing peptides can be used for peptide library construction, pull-down experiments, and structure-activity relationship studies where position-specific affinity tags are required.

3. Protein Engineering Probes

H-Lys(biotinyl)-OH finds application in protein engineering and chemical probe generation where lysine-based biotinylation supports affinity-driven workflows. The amino-acid framework can be used to design biotinylated linkers or residue analogs that maintain stereochemical identity at the lysine α-center, which can be relevant for recognition by enzymes or for maintaining conformational preferences in engineered constructs. The biotin moiety enables streptavidin-mediated immobilization, allowing controlled orientation of biomolecules for binding studies, imaging, or immobilized enzymatic assays. Downstream utility includes preparation of biotin-tagged protein reagents, affinity capture handles for proteomics workflows, and intermediate formation for immobilized biomolecule platforms.

4. Analytical Affinity Standards

H-Lys(biotinyl)-OH is applied in analytical research as a chemically defined biotin-containing reference material and calibration component for affinity-based detection formats. The compound's lysine α-carboxyl group and α-amino functionality support consistent derivatization chemistry, while the biotin ureido/thiophene-containing motif provides a strong, sequence-independent binding interaction with streptavidin or avidin. The stereochemically defined amino-acid center and the stable biotin scaffold help generate reproducible conjugates for method development, including immunoassay-like affinity capture and pull-down readouts. The compound can also serve as a starting point for preparing labeled standards used to evaluate conjugation efficiency, immobilization behavior, and assay reproducibility in biochemical measurement workflows.

5. Process Chemistry Intermediate

H-Lys(biotinyl)-OH is suitable for process chemistry intermediate preparation in fine chemical and specialty chemical production where a biotin-bearing amino-acid derivative is required for downstream manufacturing. The molecule's functional group set, including the α-amino/α-carboxyl and the biotin heteroatom-rich binding motif, supports controlled conversion into protected amino acid derivatives, activated esters, or coupling-ready forms for scale-up-compatible synthesis. The lysine side-chain attachment of biotin provides a defined substitution pattern that can reduce variability in subsequent conjugation steps compared with nonspecific biotinylation approaches. Downstream, the compound can be employed to manufacture biotinylated peptide intermediates, affinity-tagged building blocks, and industrially relevant reagents for biochemical tool production and specialty labeling chemistry.

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