In search of the chemical basis of the hemolytic potential of silicas
| Autor: | Bice Fubini, Vera Bolis, Dominique Lison, Cristina Pavan, Maura Tomatis, Virginie Rabolli, Mara Ghiazza |
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| Rok vydání: | 2013 |
| Předmět: |
Morphology (linguistics)
Erythrocytes Hot Temperature Free Radicals Surface Properties Toxicology Hemolysis Crystallinity chemistry.chemical_compound medicine Organic chemistry Humans Particle Size Fumed silica Ions Aqueous solution Chemistry General Medicine medicine.disease Silicon Dioxide Membrane Chemical engineering Siloxane Particle Crystallization Aluminum |
| Zdroj: | Chemical research in toxicology. 26(8) |
| ISSN: | 1520-5010 |
| Popis: | The membranolytic activity of silica particles toward red blood cells (RBCs) has been known for a long time and is sometimes associated with silica pathogenicity. However, the molecular mechanism and the reasons why hemolysis differs according to the silica form are still obscure. A panel of 15 crystalline (pure and commercial) and amorphous (pyrogenic, precipitated from aqueous solutions, vitreous) silica samples differing in size, origin, morphology, and surface chemical composition were selected and specifically prepared. Silica particles were grouped into six groups to compare their potential in disrupting RBC membranes so that one single property differed in each group, while other features were constant. Free radical production and crystallinity were not strict determinants of hemolytic activity. Particle curvature and morphology modulated the hemolytic effect, but silanols and siloxane bridges at the surface were the main actors. Hemolysis was unrelated to the overall concentration of silanols as fully rehydrated surfaces (such as those obtained from aqueous solution) were inert, and one pyrogenic silica also lost its membranolytic potential upon progressive dehydration. Overall results are consistent with a model whereby hemolysis is determined by a defined surface distribution of dissociated/undissociated silanols and siloxane groups strongly interacting with specific epitopes on the RBC membrane. |
| Databáze: | OpenAIRE |
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