In Situ Comparative Studies of Self-Assembly Adsorption of Bovine Serum Albumin on Nano Films by Atomic Force Microscopy

2011 ◽  
Vol 11 (12) ◽  
pp. 10765-10769 ◽  
Author(s):  
Xuesong Ye ◽  
Yong Zeng ◽  
Tao Zhou ◽  
Feng Liu ◽  
Jun Liu ◽  
...  
2012 ◽  
Vol 94 ◽  
pp. 213-219 ◽  
Author(s):  
Viliam Kolivoška ◽  
Miroslav Gál ◽  
Magdaléna Hromadová ◽  
Štěpánka Lachmanová ◽  
Hana Tarábková ◽  
...  

2008 ◽  
Vol 32 ◽  
pp. 49-52 ◽  
Author(s):  
Chun Chih Lai ◽  
John M. Bell ◽  
Nunzio Motta

A new, direct method has been developed to measure the adhesion forces of bovine serum albumin (BSA) on surfaces by using Atomic Force Microscopy (AFM) in liquid environment. We were able to measure interactions between proteins and substrate surface in PBS solution directly without any modification to the substrate or the AFM tip. Two different surfaces have been used in the experiments: mica (hydrophilic surface) and polystyrene (hydrophobic surface). The results show that a polystyrene surface is more adhesive to BSA than a mica surface. This is consistent with previous research, which assessed that hydrophobic surfaces enhance protein adhesion but hydrophilic surfaces do not, demonstrating the effectiveness of the technique.


2008 ◽  
Vol 07 (06) ◽  
pp. 299-303 ◽  
Author(s):  
CHUN-CHIH LAI ◽  
NUNZIO MOTTA ◽  
JOHN M. BELL

A novel, direct technique has been developed to measure the interactions of bovine serum albumin (BSA) on surfaces by using atomic force microscopy (AFM) in a liquid environment. We have been able to measure adhesion forces between proteins and substrate surfaces in phosphate-buffered saline (PBS) solution directly, without any modification to the substrate and the AFM tip. Two different surfaces have been used in the measurements: mica (hydrophilic surface) and polystyrene (hydrophobic surface). The results show that a polystyrene surface has larger adhesion forces to BSA than a mica surface. This is consistent with previous research, which demonstrated that hydrophobic surfaces enhance protein adhesion but hydrophilic surfaces do not.


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