Anti-Biotin polyclonal antibody [AP]

We report herein the synthesis of N-substituted indoles resulting from the ring-closing metathesis of indole precursors bearing N-terminal alkenes. The aqueous metathesis of the indole precursors gave good yields of N-substituted indoles (up to 72%) with commercial metathesis catalysts and with artificial metalloenzymes based on the biotin-streptavidin technology. Strikingly, the yield of the N-acetylindole increases in presence of a second metathesis substrate. [GRAPHICS] .

We report a molecular dynamics (MD) simulation study of protein binding at the aqueous-liquid crystal (LC) interfaces of bioconjugated mesogenic molecules. As a simple model of these interfaces, we use monolayers composed of biotin-conjugated or biotin-free amphiphilic mesogenic molecules and streptavidin in water. The all-atom MD simulations reveal that the binding of streptavidin to the biotin mesogenic monolayer is significantly stronger than that to biotin-free mesogenic monolayers. Although specific protein binding marginally increases the overall orientational order and the tilt of the biotin-conjugated mesogenic molecules of the monolayer, significant changes in tilt were observed near the bound protein (in contrast to the protein interaction with the monolayer without biotin). We also observe that specific protein binding changes the dynamic properties of the mesogens within the monolayer (e.g., lateral diffusion coefficients) and associated water. Overall, these MD simulations advance our understanding of the molecular-level phenomena involved in the binding of biomolecules and subsequent dynamic changes at the aqueous-LC interfaces. These results provide guidance to future molecular-level designs of biofunctional LC interfaces.