A phospholipid monolayer was prepared at the air-water interface and different amounts of a lipid-tagged genetically fragmented antibody were incorporated into the lipid matrix. The molecular surface area of the film increased with antibody concentration and reached a maximum at an antibody mole fraction of 0.03. Atomic force microscopy showed that the antibody fragment was segregated into protein-rich domains with a mean diameter of about 12 nm. In-situ measurements with surface plasmon resonance displayed a specific binding of antigen—a binding that was not observed to the pure lipid film.
|Journal||Thin Solid Films|
|Publication status||Published - 1996|
|MoE publication type||A1 Journal article-refereed|
|Event||Seventh International Conference on Organized Molecular Films - Numana, Italy|
Duration: 10 Sep 1995 → 15 Sep 1995
Vikholm, I., & Peltonen, J. (1996). Layer formation of a lipid-taged single-chain antibody and the interaction with antigen. Thin Solid Films, 284-285, 924-926. https://doi.org/10.1016/S0040-6090(95)08481-9