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Quantitative proteomics analysis of adsorbed plasma proteins classifies nanoparticles with different surface properties and size
Author(s) -
Zhang Haizhen,
Burnum Kristin E.,
Luna Maria L.,
Petritis Brianne O.,
Kim JongSeo,
Qian WeiJun,
Moore Ronald J.,
HerediaLangner Alejandro,
WebbRobertson BobbieJo M.,
Thrall Brian D.,
Camp David G.,
Smith Richard D.,
Pounds Joel G.,
Liu Tao
Publication year - 2011
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100037
Subject(s) - proteomics , nanoparticle , quantitative proteomics , chemistry , blood proteins , biocompatibility , nanotechnology , chromatography , materials science , biochemistry , organic chemistry , gene
Nanoparticle biological activity, biocompatibility and fate can be directly affected by layers of readily adsorbed host proteins in biofluids. Here, we report a study on the interactions between human blood plasma proteins and nanoparticles with a controlled systematic variation of properties using 18 O‐labeling and LC‐MS‐based quantitative proteomics. We developed a novel protocol to both simplify isolation of nanoparticle bound proteins and improve reproducibility. LC‐MS analysis identified and quantified 88 human plasma proteins associated with polystyrene nanoparticles consisting of three different surface chemistries and two sizes, as well as, for four different exposure times (for a total of 24 different samples). Quantitative comparison of relative protein abundances was achieved by spiking an 18 O‐labeled “universal” reference into each individually processed unlabeled sample as an internal standard, enabling simultaneous application of both label‐free and isotopic labeling quantification across the entire sample set. Clustering analysis of the quantitative proteomics data resulted in distinctive patterns that classified the nanoparticles based on their surface properties and size. In addition, temporal data indicated that the formation of the stable protein corona was at equilibrium within 5 min. The comprehensive quantitative proteomics results obtained in this study provide rich data for computational modeling and have potential implications towards predicting nanoparticle biocompatibility.