Sequential adsorption of bacteriophage T4 lysozyme stability variants at solid–water interfaces

• Published in: Colloids and surfaces, B, Biointerfaces Vol. 27; no. 4; pp. 277 - 285
• Main Authors: Podhipleux, N, McGuire, J, Bothwell, M.K, Horbett, T.A
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01-03-2003
• Subjects: Bacteriophage T4 lysozyme; Sequential adsorption; Synthetic stability mutants; Synthetic stability mutants; Bacteriophage T4 lysozyme; Sequential adsorption
• ISSN: 0927-7765; 1873-4367
• DOI: 10.1016/S0927-7765(02)00050-4

The sequential adsorption of the wild type T4 lysozyme and one of its structural stability variants was studied, using ellipsometry and
125I radioisotope labeling techniques. The mutant lysozyme was produced by substitution of the isoleucine residue at position 3 in the wild type with a tryptophan residue, resulting in a protein with lower structural stability. The mutant protein was more resistant to surfactant-mediated elution, and apparently adsorbed at the interfaces with a greater interfacial area/molecule than the wild typeT4 lysozyme. However, the results of each type of experiment suggested that sequential adsorption and exchange of proteins occurred only in the case of the less stable mutant followed by the wild type. This suggests that, in these exchange reactions, properties of the adsorbing protein (e.g. its ability to adsorb when a relatively small amount of unoccupied area is present) were more important than the apparent binding strength of the adsorbed protein molecules.