Reasearchers at the New Jersey Center for Biomaterials recently analyzed horseradish peroxidase (HRP) tethering on to biotinylated E1001 (1K) scaffolds. Biotin is attached to scaffold and protein alike as a method to increase binding ability. Streptavidin, a protein taken from the Streptomyces avidinii bacteria, was used as a binding agent between the HRP and the scaffold due to its stability and extraordinarily high affinity for biotin. By adding the streptavidin to the biotinylated scaffold, then adding the bHRP, the researchers hoped to create a stable system.
However, it was found that the specific activity of biotinylated horseradish peroxidase (bHRP) was less than its non-biotinylated counterpart. The researchers concluded that biotin could have an effect on HRP’s activity and postulate that binding sites of biotin may be closer to the active center. They acknowledge that the number of biotin molecules and the biotin binding sites on the HRP peptide chain can not be determined and may require further research.