Interaction of metal oxide nanoparticles with lung surfactant protein A |
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Authors: | Christine Schulze |
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Affiliation: | a Department of Biopharmaceutics and Pharmaceutical Technology, Saarland University, Saarbruecken, Germany b BASF SE, Polymer Physics Research, GKP/O - G201, Ludwigshafen, Germany c Department of Drug Delivery (DDEL) Helmholtz-Institute for Pharmaceutical Research Saarland (HIPS) Helmholtz Center for Infection Research (HZI), Saarland University, Campus A 4 1, Saarbruecken, Germany |
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Abstract: | The alveolar lining fluid (ALF) covering the respiratory epithelium of the deep lung is the first biological barrier encountered by nanoparticles after inhalation. We here report for the first time significant differences for metal oxide nanoparticles to the binding of surfactant protein A (SP-A), the predominant protein component of ALF. SP-A is a physiologically most relevant protein and provides important biological signals. Also, it is involved in the lung’s immune defence, controlling e.g. particle binding, uptake or transcytosis by epithelial cells and macrophages. In our study, we could prove different particle-protein interaction for eight different nanoparticles, whereas particles of the same bulk material revealed different adsorption patterns. In contrast to other proteins as bovine serum albumin (BSA), SP-A does not seem to significantly deagglomerate large agglomerates of particles, indicating different adsorption mechanisms as in the well-investigated model protein BSA. These findings may have important consequences for biological fate and toxicological effects of inhaled nanomaterials. |
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Keywords: | ALF, alveolar lining fluid SP-A, surfactant protein A BSA, bovine serum albumin pBALF, porcine broncheoalveolar lavage fluid BCA assay, bicinchinoninic acid protein quantification assay AUC, analytical ultracentrifugation CRD, carbohydrate recognition domains SDS-PAGE, sodiumdodecylsulfate-polyacryl-gelelectrophoresis SPs, surfactant proteins FCS, fetal calf serum CNTs, carbonanotubes |
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