Atomic force microscopy study of the adsorption of protein molecules on transferred Langmuir monolayer
| Autor: | A. L. Tolstikhina, N. D. Stepina, R. V. Gaĭnutdinov, N. N. Novikova, E. A. Yur’eva, Albert K. Khripunov |
|---|---|
| Rok vydání: | 2010 |
| Předmět: |
chemistry.chemical_classification
Langmuir Silicon technology industry and agriculture chemistry.chemical_element Substrate (chemistry) Nanotechnology General Chemistry Polymer Condensed Matter Physics chemistry.chemical_compound Adsorption chemistry Chemical engineering Dipalmitoylphosphatidylcholine Monolayer Deposition (phase transition) lipids (amino acids peptides and proteins) General Materials Science |
| Zdroj: | Crystallography Reports. 55:849-853 |
| ISSN: | 1562-689X 1063-7745 |
| DOI: | 10.1134/s1063774510050251 |
| Popis: | Ordered protein films have been obtained by the adsorption of protein molecules on a Langmuir monolayer, which had previously formed on a silicon substrate, using the Langmuir-Blodgett and molecular self-organization methods. A mixture of cholesterol with dipalmitoylphosphatidylcholine (DPPC) and a polymer—cellulose acetopivalinate—were used as immobilization materials. Protein molecules (catalase and alkaline phosphatase) immobilized on solid substrates have been investigated by atomic force micros-copy. It was shown that the developed combined technique provides a deposition of homogeneous ultrathin protein films with a high degree of filling. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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