Open AccessEnhancing Surface Capture and Sensing of Proteins with Low-Power Optothermal Bubbles in a Biphasic Liquid
Author(s) -
Youngsun Kim,
Hongru Ding,
Yuebing Zheng
Publication year - 2020
Publication title -
nano letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.853
H-Index - 488
eISSN - 1530-6992
pISSN - 1530-6984
DOI - 10.1021/acs.nanolett.0c01969
Subject(s) - bubble , microbubbles , aqueous solution , biosensor , surface modification , liquid bubble , nanotechnology , materials science , chemical physics , chemistry , molecular binding , microfluidics , chemical engineering , molecule , chromatography , mechanics , organic chemistry , physics , acoustics , engineering , ultrasound
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.