Interactions between bovine serum albumin layers adsorbed on different substrates measured with an atomic force microscope

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.

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Effect of pH on the Formation of a Bovine Serum Albumin Layer on a Poly(stryren-co-maleic Acid) Surface

Advanced Materials Research ◽

10.4028/www.scientific.net/amr.93-94.583 ◽

2010 ◽

Vol 93-94 ◽

pp. 583-586 ◽

Cited By ~ 2

Author(s):

Tippavan Hongkachern ◽

Verawat Champreda ◽

Toemsak Srikhirin ◽

Thidarat Wangkam ◽

Tanakorn Osotchan

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Maleic Acid ◽

Bovine Serum ◽

Quartz Crystal ◽

Ph Value ◽

Layer Formation ◽

Force Microscopy ◽

Ph Values ◽

Atomic Force

The layer formation of bovine serum albumin (BSA) on a poly(styrene-co-maleic acid) (PSMA) surface was investigated by using quartz crystal microbalance (QCM) technique at various pH values. The formation of a BSA surface was examined by atomic force microscopy (AFM). To study the effect on the layer formation, the pH of solution was varied from 2 to 7.4 while the concentration of BSA was in the range of 0.01 to 5 mg/ml during the layer absorption. It was found that the BSA adsorption strongly depends on the pH of solution, and the concentration of BSA. The absorption layer occurred maximum at the pH value of 3.5 which resulted from the charge of PSMA and BSA molecules. The layer formation reached the saturate value at the concentration higher than 3 mg/ml. The molecular packing of the BSA layer at different pH values was determined by AFM and total mass change of QCM.

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Penetration of Bovine Serum Albumin into Dipalmitoylphosphatidylglycerol Monolayers: Direct Observation by Atomic Force Microscopy

Chemical and Pharmaceutical Bulletin ◽

10.1248/cpb.53.42 ◽

2005 ◽

Vol 53 (1) ◽

pp. 42-47 ◽

Cited By ~ 10

Author(s):

Isao Ohtsuka ◽

Shoko Yokoyama

Keyword(s):

Atomic Force Microscopy ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Direct Observation ◽

Bovine Serum ◽

Force Microscopy ◽

Atomic Force

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ATOMIC FORCE MICROSCOPY MEASUREMENTS OF BOVINE SERUM ALBUMIN ADHESION FORCES ON SURFACES

International Journal of Nanoscience ◽

10.1142/s0219581x08005468 ◽

2008 ◽

Vol 07 (06) ◽

pp. 299-303 ◽

Cited By ~ 6

Author(s):

CHUN-CHIH LAI ◽

NUNZIO MOTTA ◽

JOHN M. BELL

Keyword(s):

Atomic Force Microscopy ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Hydrophobic Surface ◽

Adhesion Forces ◽

Liquid Environment ◽

Force Microscopy ◽

Atomic Force ◽

Direct Technique

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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