Manufactured oxide nanoparticles (NPs) have large production and widespread applications, which will inevitably enter the environment. NPs can interact with proteins in living beings due to the fact that NPs can transport into blood or across cell membranes into cells. Conformational change of protein molecules after sorption on oxide NPs has been reported. Therefore, it is important to understand the adsorption mechanism of protein onto oxide NPs surfaces. Although few works have reported protein adsorption behaviors, a general systematic comparison of the effects of particle size and surface groups on protein adsorption by widely studied NPs still needs to be made. Moreover, the relationship between adsorption maxima, which are related to protein conformational change and particle toxicity, and protein conformational change has not yet been studied. Therefore, in this work, the adsorption behavior of bovine serum albumin (BSA) protein on three types of nano oxide particles (viz., TiO2, SiO2, and Al2O3) was investigated in order to explore their interaction mechanisms, compared with that on regular bulk particles (BPs). The BSA adsorption maxima on oxide particles were regulated by the surface area of oxide particles. BSA adsorption was primarily induced by electrostatic attraction and ligand exchange between BSA and oxide surfaces. Surface hydrophilicity, surface charge and aggregation of oxide particles also affected their adsorption of BSA. Calculations suggested that a multilayer of BSA covered α-Al2O3, and single layer covered the other oxide particle surfaces. Primary structures of BSA molecules were adsorbed and changed on surfaces of oxide particles.
| Identifer | oai:union.ndltd.org:UMASS/oai:scholarworks.umass.edu:theses-1475 |
| Date | 01 January 2010 |
| Creators | Song, Lei |
| Publisher | ScholarWorks@UMass Amherst |
| Source Sets | University of Massachusetts, Amherst |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Masters Theses 1911 - February 2014 |
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