Enhancing Surface Capture and Sensing of Proteins with Low-Power Optothermal Bubbles in a Biphasic Liquid.

Abstract

Molecular binding in surface-based biosensing is inherently governed by diffusional transport of molecules in solution to surface-immobilized counterparts. Optothermally generated surface microbubbles can quickly accumulate solutes at the bubble-liquid-substrate interface due to high-velocity fluid flows. Despite its potential as a concentrator, however, the incorporation of bubbles into protein-based sensing is limited by high temperatures. Here, we report a biphasic liquid system, capable of generating microbubbles at a low optical power/temperature by formulating PFP as a volatile, water-immiscible component in the aqueous host. We further exploited zwitterionic surface modification to prevent unwanted printing during bubble generation. In a single protein-protein interaction model, surface binding of dispersed proteins to capture proteins was enhanced by 1 order of magnitude within 1 min by bubbles, compared to that from static incubation for 30 min. Our proof-of-concept study exploiting fluid formulation and optothermal add-on paves an effective way toward improving the performances of sensors and spectroscopies.