Biotin, also called vitamin H, is a coenzyme that participates in the metabolism of fatty acids, leucine, and glucose. It binds noncovalently to streptavidin and avidin with high affinity and specificity. The avidin–biotin interaction is the strongest noncovalent protein–ligand binding force known (Ka=1015 M-1). The avidin–biotin interaction has been widely explored in biotechnology for protein purification and detection. The process of attaching biotin or a biotin analog to a biomolecule is called biotinylation. A very hydrophobic molecule, biotin has to be dissolved in organic solvent prior to any bioconjugation reaction in aqueous buffer. Furthermore, excessive biotinylation of a biomolecule, such as protein, can cause aggregation. There are a variety of ways to control the biotinylation of proteins. The carboxyl group of the biotin is usually modified to suit conjugation needs without affecting biotin function.
At CellMosaic, we routinely perform biotinylation of a variety of biomolecules with or without linkers. We can help customers with any of their biotinylation requirements. For custom biotinylation, please contact us for a quote.
Example: Clean synthesis of a biotinylated peptide on solid phase at CellMosaic.
Melting point: 232 - 233 °C
Solubility at 25°C in water: ~ 0.22 mg/mL
pH of a 0.01% aqueous solution: 4.5