Nanobubbles on solid surface imaged by atomic force microscopy

Author(s):  
Shi-Tao Lou ◽  
Zhen-Qian Ouyang ◽  
Yi Zhang ◽  
Xiao-Jun Li ◽  
Jun Hu ◽  
...  
2017 ◽  
Vol 53 (98) ◽  
pp. 13172-13175 ◽  
Author(s):  
Keito Koizumi ◽  
Masaaki Akamatsu ◽  
Kenichi Sakai ◽  
Shinya Sasaki ◽  
Hideki Sakai

A solubilization-induced morphological change in surfactant surface aggregates was imaged in real-time, using high-speed atomic force microscopy.


2005 ◽  
Vol 899 ◽  
Author(s):  
Abhinandan Agrawal ◽  
Gareth H. McKinley

AbstractThe formation of nanobubbles at solid-liquid interfaces has been studied using the atomic force microscopy (AFM) imaging technique. Nanobubble formation strongly depends on both the hydrophobicity of the solid surface and the polarity of the liquid subphase. While nanobubbles do not form on flat hydrophilic (silicon oxide wafer) surfaces immersed in water, they appear spontaneously at the interface of water against smooth, hydrophobic (silanized wafer) surfaces. From the experimental observations we draw the conclusion that the features observed in the AFM images are deformable, air-filled bubbles. In addition to the hydrophobicity of the solid surface, differences in solubility of air between two miscible fluids can also lead to formation of nanobubbles. We observe that nanobubbles appear at the interface of water against hydrophilic silicon oxide surfaces after in-situ mixing of ethanol and water in the fluid-cell.The shapes of the nanobubbles are well approximated by spherical caps, with width much larger than the height of the caps. We quantify the morphological distribution of nanobubbles by evaluating several important bubble parameters including surface coverage and radii of curvature. In conjunction, with an analytical model available in the literature, we use this information to estimate that the present nanobubble morphology may give rise to slip lengths ∼1–2 µm in pressure driven flows for water flowing over the hydrophobic surface. The consistency of the calculated slip length with the experimental values reported in the literature, suggests that the apparent fluid slip observed experimentally at hydrophobic surfaces may arise from the presence of nanobubbles.


2010 ◽  
Vol 257 (2) ◽  
pp. 558-564 ◽  
Author(s):  
Huizhen Yuan ◽  
Wenping Lian ◽  
Yonghai Song ◽  
Shouhui Chen ◽  
Lili Chen ◽  
...  

2005 ◽  
Vol 187 (6) ◽  
pp. 2127-2137 ◽  
Author(s):  
Brian H. Lower ◽  
Ruchirej Yongsunthon ◽  
F. Paul Vellano ◽  
Steven K. Lower

ABSTRACT All microbial biofilms are initiated through direct physical contact between a bacterium and a solid surface, a step that is controlled by inter- and intramolecular forces. Atomic force microscopy and confocal laser scanning microscopy were used simultaneously to observe the formation of a bond between a fluorescent chimeric protein on the surface of a living Escherichia coli bacterium and a solid substrate in situ. The chimera was composed of a portion of outer membrane protein A (OmpA) fused to the cyan-fluorescent protein AmCyan. Sucrose gradient centrifugation and fluorescent confocal slices through bacteria demonstrated that the chimeric protein was targeted and anchored to the external cell surface. The wormlike chain theory predicted that this protein should exhibit a nonlinear force-extension “signature” consistent with the sequential unraveling of the AmCyan and OmpA domains. Experimentally measured force-extension curves revealed a unique pair of “sawtooth” features that were present when a bond formed between a silicon nitride surface (atomic force microscopy tip) and E. coli cells expressing the OmpA-AmCyan protein. The observed sawtooth pair closely matched the wormlike chain model prediction for the mechanical unfolding of the AmCyan and OmpA substructures in series. These sawteeth disappeared from the measured force-extension curves when cells were treated with proteinase K. Furthermore, these unique sawteeth were absent for a mutant stain of E. coli incapable of expressing the AmCyan protein on its outer surface. Together, these data show that specific proteins exhibit unique force signatures characteristic of the bond that is formed between a living bacterium and another surface.


Sign in / Sign up

Export Citation Format

Share Document