Fluorescent Biotin Analogues for Microstructure Patterning and Selective Protein Immobilization

Abstract

Benzyl substitution on ureido nitrogens of biotin led to manifestation of aggregation-induced emission, which was studied by steady-state fluorescence, microscopy, and TD-DFT, providing a rationale into the observed photophysical behavior. Besides exhibiting solvatochromism, the biotin derivatives revealed emission peaks centered at ∼430 and 545 nm, which has been attributed to the π-π stacking interactions. Our TD-DFT results also correlate the spectroscopic data and quantify the nature of transitions involved. The isothermal titration calorimetry data substantiates that the binding of the biotin derivatives with avidin are pretty strong. These derivatives on lithographic patterning present a platform for site specific strept(avidin) immobilization, thus opening avenues for potential applications exploiting these interactions. The fluorescent biotin derivatives can thus find applications in cellular biology and imaging.

A versatile platform for surface modification of microfluidic droplets

“…organic solvent and extreme pH) and elevated temperature. 32 There are three main types of biotin-binding glycoproteins: avidin, streptavidin and NeutrAvidin. Compared with avidin and streptavidin, NeutrAvidin is a much more ideal biotin-binding reagent because it has the highest specificity.…”