Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10377671 | Journal of Colloid and Interface Science | 2005 | 8 Pages |
Abstract
The interactions of human insulin, Zn-free human insulin, and AspB28 insulin with a hydrophobic surface were studied by ellipsometry. All three insulin types investigated adsorbed with high affinity onto the hydrophobic surface, as the plateau of the adsorption isotherm, represented by the irreversible bound fraction, was reached at concentrations >10â3 mg/ml. The plateau values for human insulin and Zn-free human insulin could not be distinguished with statistical significance, whereas the plateau value for AspB28 insulin was lower than those for the two others, with an adsorbed amount corresponding to a monolayer of insulin monomers. The results observed may be explained by differences in self-association patterns of the insulin types or by enhanced charge repulsion between the AspB28 analog and the negatively charged surface.
Related Topics
Physical Sciences and Engineering
Chemical Engineering
Colloid and Surface Chemistry
Authors
S.H. Mollmann, J.T. Bukrinsky, S. Frokjaer, U. Elofsson,