A new insight into the adsorption of bovine serum albumin onto porous polyethylene membrane by zeta potential measurements, FTIR analyses, and AFM observations

The mode of adsorption of bovine serum albumin (BSA) on porous polyethylene (PE) membrane was studied as a function of time and concentration, which may contribute to the surface coverage. An improved physical model for adsorption is initiated based on the results of the adsorptional and desorptiona...

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Published inJournal of colloid and interface science Vol. 262; no. 2; pp. 342 - 350
Main Authors Xu, Tongwen, Fu, Rongqiang, Yan, Lifeng
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 15.06.2003
Elsevier
Subjects
Adsorption
AFM
Animals
Biological and medical sciences
Bovine serum albumin
Electrodes
FTIR
Fundamental and applied biological sciences. Psychology
Membranes, Artificial
Microscopy, Atomic Force
Molecular and cellular biology
Polyethylene
Porosity
Protein Binding
Serum Albumin, Bovine - chemistry
Spectroscopy, Fourier Transform Infrared
Zeta potential
AFM
Bovine serum albumin
Adsorption
Zeta potential
FTIR
Genetics
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Summary:The mode of adsorption of bovine serum albumin (BSA) on porous polyethylene (PE) membrane was studied as a function of time and concentration, which may contribute to the surface coverage. An improved physical model for adsorption is initiated based on the results of the adsorptional and desorptional measurements, FTIR analysis, and AFM observations as well as streaming potential measurements. The results obtained indicate that the adsorptional mode depend on both time and concentration. It is shown that a critical concentration (about 1000 ppm here) exists in the adsorptional process. Below this concentration, the adsorption seems to be conducted in a normal side-on way but time elapse gives rise to greater conformational change than concentration increase; above this concentration, the aggregation of protein molecular plays a decisive role and the adsorption is in an aggregation way, which is similar to end-on, but a relative large gap between the adsorbed molecules exists due to aggregation. This conclusion is general and can be expected to apply in other globular protein–hydrophobic porous surface systems.
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ISSN:0021-9797
1095-7103
DOI:10.1016/S0021-9797(03)00208-X