2014
DOI: 10.1007/s12274-013-0400-0
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Quantitative study of protein coronas on gold nanoparticles with different surface modifications

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Cited by 90 publications
(97 citation statements)
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“…The results showed that there is negligible protein adsorption on the surface of PEG-Au NPs. Fibrinogen can induce NP aggregation when it interacts with other non-PEG-coated Au NPs, while citrate or thioglycolic acid-coated Au NPs are capable of adsorbing TRF and BSA to form a 6–8 nm thickness corona [81]. The molecular weight of PEG ligands on Au NPs also influenced the bound proteins.…”
Section: Au Np–protein Interactionsmentioning
confidence: 99%
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“…The results showed that there is negligible protein adsorption on the surface of PEG-Au NPs. Fibrinogen can induce NP aggregation when it interacts with other non-PEG-coated Au NPs, while citrate or thioglycolic acid-coated Au NPs are capable of adsorbing TRF and BSA to form a 6–8 nm thickness corona [81]. The molecular weight of PEG ligands on Au NPs also influenced the bound proteins.…”
Section: Au Np–protein Interactionsmentioning
confidence: 99%
“…TEM and DLS are widely used to measure the thickness of the protein corona on NPs in dried samples and in an aqueous solution, respectively. Au NPs with different modifications can interact with BSA and the hydrodynamic diameter or protein thickness increases determined by DLS and TEM [81]. Moreover, UV–vis–NR spectra can detect significant shifts in the peak position of the SPR of Au NPs before and after protein adsorption.…”
Section: Au Np–protein Interactionsmentioning
confidence: 99%
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“…13,35,36,45 Bare nanoparticles are unable to survive within a biological system since they are immediately covered by a layer of proteins from the fluid which forms the hard protein corona and which continues to grow until they attain a stable state, which is often a long-term process as observed in the case of SiQD 1050. 13,35,36,45 Bare nanoparticles are unable to survive within a biological system since they are immediately covered by a layer of proteins from the fluid which forms the hard protein corona and which continues to grow until they attain a stable state, which is often a long-term process as observed in the case of SiQD 1050.…”
Section: Page 17 Of 23 Rsc Advancesmentioning
confidence: 99%
“…CD spectroscopy uses changes in the chiral properties of a protein to predict changes in its secondary structure. Measured interactions between plasma proteins and NPs can be quantified using several kinetic models and equations (38)(39)(40). All the methods described in Table 2 are quite accessible and straightforward to evaluate nano-bio interface in pure water or a simple buffer system.…”
Section: Figure 3 Active Interactions At the Nano-bio Interface [Inspmentioning
confidence: 99%