IgG and fibrinogen driven nanoparticle aggregation
| Autor: | Risto Cukalevski, Christopher J.R. Dunning, Tord Berggård, Tommy Cedervall, Silvia A. Ferreira |
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| Přispěvatelé: | Universidade do Minho |
| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
Low protein
02 engineering and technology 010402 general chemistry Fibrinogen 01 natural sciences Immunoglobulin G Protein–protein interaction Aggregation Dynamic light scattering In vivo medicine Immunoglobulin General Materials Science Electrical and Electronic Engineering Science & Technology biology Chemistry Protein Nanoparticles (NPs) 021001 nanoscience & nanotechnology Condensed Matter Physics Blood proteins Atomic and Molecular Physics and Optics 0104 chemical sciences Biochemistry Drug delivery biology.protein Corona 0210 nano-technology medicine.drug |
| Zdroj: | Repositório Científico de Acesso Aberto de Portugal Repositório Científico de Acesso Aberto de Portugal (RCAAP) instacron:RCAAP |
| Popis: | A thorough understanding of how proteins induce nanoparticle (NP) aggregation is crucial when designing in vitro and in vivo assays and interpreting experimental results. This knowledge is also crucial when developing nano-applications and formulation for drug delivery systems. In this study, we found that extraction of immunoglobulin G (IgG) from cow serum results in lower polystyrene NPs aggregation. Moreover, addition of isolated IgG or fibrinogen to fetal cow serum enhanced this aggregation, thus demonstrating that these factors are major drivers of NP aggregation in serum. Counter-intuitively, NP aggregation was inversely dependent on protein concentration; i.e., low protein concentrations induced large aggregates, whereas high protein concentrations induced small aggregates. Protein-induced NP aggregation and aggregate size were monitored by absorbance at 400 nm and dynamic light scattering, respectively. Here, we propose a mechanism behind the protein concentration dependent aggregation; this mechanism involves the effects of multiple protein interactions on the NP surface, surface area limitations, aggregation kinetics, and the influence of other serum proteins. We thank Professor Sara Linse for scientific discussions and advice and Professor Patrik Brundin for enabling access to the light microscope. The project received financial support from Nanometer structure consortium at Lund University (nmC@LU), Lars Hierta Foundation, and the research school FLAK of Lund University. |
| Databáze: | OpenAIRE |
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