Abstract
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.
| Original language | English |
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| Pages (from-to) | 924-926 |
| Journal | Thin Solid Films |
| Volume | 284-285 |
| DOIs | |
| Publication status | Published - 1996 |
| MoE publication type | A1 Journal article-refereed |
| Event | Seventh International Conference on Organized Molecular Films - Numana, Italy Duration: 10 Sept 1995 → 15 Sept 1995 |