Magnetite Nanoparticles Biomineralization in the Presence of the Magnetosome Membrane Protein MamC: Effect of Protein Aggregation and Protein Structure on Magnetite Formation
| Autor: | Alejandro B. Rodríguez-Navarro, Salvador Casares Atienza, Ana I. Azuaga Fortes, Rafael Lopez-Moreno, Carmen Valverde-Tercedor, Antonia Fernández-Vivas, Raz Zarivach, Concepcion Jimenez-Lopez |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Magnetosome 02 engineering and technology General Chemistry Protein aggregation 021001 nanoscience & nanotechnology Condensed Matter Physics 03 medical and health sciences chemistry.chemical_compound 030104 developmental biology Protein structure chemistry Membrane protein Biochemistry Protein purification Biophysics General Materials Science 0210 nano-technology Integral membrane protein Biomineralization Magnetite |
| Zdroj: | Crystal Growth & Design. 17:1620-1629 |
| ISSN: | 1528-7505 1528-7483 |
| DOI: | 10.1021/acs.cgd.6b01643 |
| Popis: | MamC from Magnetococcus marinus MC-1 has been shown to control the size of magnetite crystals in in vitro experiments, thereby demonstrating its potential as a candidate protein for the production of magnetite nanoparticles possibly useful in medical and other applications. However, the importance of the structure and aggregation state of the protein on the resulting biomimetic nanoparticles has not yet been assessed. One method normally used to prevent the aggregation of integral membrane proteins is the introduction of detergents during protein purification. In this study, results from protein aggregation following the addition of Triton-X100, DDM, and LDAO are presented. Magnetite particles formed in the presence of MamC purified using these three detergents were compared. Our results show that detergents alter the structure of the folded recombinant protein, thus preventing the ability of MamC to control the size of magnetite crystals formed chemically in vitro. Furthermore, we show that the introduct... |
| Databáze: | OpenAIRE |
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