Bovine serum albumin adsorption on nano-rough platinum surfaces studied by QCM-D
The adsorption of bovine serum albumin (BSA) on platinum surfaces with a root-mean-square roughness ranging from 1.49 nm to 4.62 nm was investigated using quartz crystal microbalance with dissipation (QCM-D). Two different BSA concentrations, 50 μg/ml and 1 mg/ml, were used, and the adsorption studi...
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Published in | Colloids and surfaces, B, Biointerfaces Vol. 66; no. 1; pp. 53 - 59 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
Elsevier B.V
01.10.2008
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Subjects | |
Online Access | Get full text |
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Summary: | The adsorption of bovine serum albumin (BSA) on platinum surfaces with a root-mean-square roughness ranging from 1.49
nm to 4.62
nm was investigated using quartz crystal microbalance with dissipation (QCM-D). Two different BSA concentrations, 50
μg/ml and 1
mg/ml, were used, and the adsorption studies were complemented by monitoring the antibody interaction with the adsorbed BSA layer. The adsorption process was significantly influenced by the surface nano-roughness, and it was observed that the surface mass density of the adsorbed BSA layer is enhanced in a non-trivial way with the surface roughness. From a close examination of the energy dissipation vs. frequency shift plot obtained by the QCM-D technique, it was additionally observed that the BSA adsorption on the roughest surface is subject to several distinct adsorption phases revealing the presence of structural changes facilitated by the nano-rough surface morphology during the adsorption process. These changes were in particular noticeable for the adsorption at the low (50
μg/ml) BSA concentration. The results confirm that the nano-rough surface morphology has a significant influence on both the BSA mass uptake and the functionality of the resulting protein layer. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0927-7765 1873-4367 |
DOI: | 10.1016/j.colsurfb.2008.05.010 |