Concentration and composition of the protein corona as a function of incubation time and serum concentration: an automated approach to the protein corona

Interaction of Iron Oxide Nanoparticles with Macrophages Is Influenced Distinctly by “Self” and “Non-Self” Biological Identities

“…More detailed profiling revealed that the α-2-HS-glycoprotein, also known as fetuin-A (FetA: 4.27-fold, 4.40-fold, and 4.03-fold enrichment), antithrombin-III (ATIII: 3.19-fold, 2.75-fold, 3.13-fold enrichment) and serum albumin (2.84-fold, 2.75-fold, 2.95-fold enrichment) were the three most abundant proteins on the PC derived from FBS and deposited on APS-, DEX-, and DMSA-IONPs, respectively (Figure D, top). Notably, the abundance of both α-2-HS-glycoprotein (AHSG) and serum albumin in the FBS-derived PC might reflect the relative abundance of these proteins in FBS, as demonstrated previously, where they represent 26.26 and 35.69% of all proteins, respectively.…”

“…Although enormous efforts have been made to better understand PC formation in relation to synthetic identity, most studies focused only on one physiological fluid at a time, neglecting the influence of the origin of the biological fluid on PC dynamics and composition. Most studies of the PC are carried out in vitro , primarily using FBS as it is a common in vitro cell culture supplement, , although some addressed PC dynamics when generated in HS, , mouse serum (MS), , or alveolar fluid, or in media containing only one kind of protein . However, no transverse studies have been performed in which the same IONPs are maintained in sera of different origins with a view to understanding how the origin of the sera influences the biological identity of IONPs and their physiological behavior.…”

Interaction of TiO2 nanoparticles with lung fluid proteins and the resulting macrophage inflammatory response

“…Gel electrophoresis was used to visualize individual proteins present in the corona of the NPs, as previously described. 30 The protein coronas were removed from the NPs by suspending the NPs in loading buffer (Laemmli, #BP-110R; Boston BioProducts, Ashland, MA), incubating for at least 5 min at 95 °C, and then loaded onto a gel (tris-glycine sodium dodecyl sulfate (SDS) gel, #4561093, Bio-Rad, Hercules, CA) for SDS-polyacrylamide gel electrophoresis (PAGE; 230 V, 35 min). A 10 to 250 kDa molecular weight marker (Precision Plus Protein Dual Color Standards, #1610374, Bio-Rad) was Environmental Science: Nano Paper included.…”

“…Proteomic analysis was carried out in the Proteomics and Metabolomics Core Facility, part of the Duke Center for Genomics and Computational Biology, as previously described. 30,31 In brief, digested samples were analyzed using LC-MS/MS with ≤500 ng of digested protein injected. NanoFlow LC was performed with an ultra-performance liquid chromatography (UPLC, 75 μm × 250 mm, nanoAcquity, Waters Corporation; 400 nL min −1 ) column and a 60 minute total elution time.…”

“…8,[20][21][22][23][24][25][26] The specific proteins that adsorb on the NP surface determine the subsequent interactions of the NP with cells and organs including cellular internalization, immune response, biodistribution, and circulation time. 22,24,25,[27][28][29] The majority of research on the protein corona, including our own, [30][31][32] has focused on blood serum proteins relevant to nanomedicines. In comparison, inhalation of NPs brings the NPs into contact with the more complex environment of lung lining fluid.…”