Research Capabilities
Proteomic Methods and QSAR Models to Predict Nanoparticle Surface Chemistry Interactions
Using advanced mass spectrometry (MS) based proteomics capabilities will provide comprehensive and accurate analysis of differential protein binding of nanomaterials in relevant biofluids and information-rich datasets that are necessary for development of quantitative structure activity relationship modeling.
Biocompatibility of nanomaterials is now a serious bottleneck in the rapidly growing fields of nanomedicine and nanotoxicology. We propose to test the hypothesis that differences in disposition and biocompatibility of different nanomaterials in biological systems will be reflected by quantitative and qualitative differences in the pattern of proteins that bind to the nanomaterials surfaces. We propose to develop proteomics approaches to measure both the abundance and stoichiometry of nanomaterial-associated proteins, and mathematical models to predict protein binding properties of the nanomaterials based upon their surface physical and chemical properties. Our proposed approach will employ a dual quantitation strategy (18O labeling and label free) to measure differential binding of proteins in biofluid to nanomaterials. The accurate mass, liquid chromatography elution time and tandem mass spectrum obtained by the hybrid high mass resolution mass spectrometer will be used for accurate peptide/protein identification and quantitation. Quantitative structure activity relationship (QSAR) modeling will be employed to formalize the physical-chemical and surface properties of nanomaterials which determine the initial interaction of nanomaterials with proteins in biofluid.