2020
DOI: 10.7150/thno.42114
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Gadolinium-doped Au@prussian blue nanoparticles as MR/SERS bimodal agents for dendritic cell activating and tracking

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Cited by 33 publications
(40 citation statements)
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“…Specifically, BSA shows seven characteristic peaks at 617, 650, 1219, 1355, 1499, 1522, and 1650 cm –1 , which could be attributed to C–C twisting, OH out-of-plane bending, the amine III of proteins, tryptophan, CC stretching in a benzenoid ring, carotene, and amide I, respectively. These peaks are almost missing in the case of LYS and OVA. Six peaks that were observed in SERS spectra of OVA are assigned to tryptophan, collagen, d­(CH), υs COO – (IgG), CC stretching in benzenoid ring, and protein amide I absorption from left to right, respectively. SERS features from LYS were also distinguishable from two other proteins. They are dominated by the bands of amino acids, such as the C–S stretching mode of cysteine, proline, phenylalanine, tyrosine, and amide I band of proteins, due to CO stretching (at 653, 825, 1032, 1164, and 1600 cm –1 , respectively). , These differences may be correlated with different amino acid species and protein spatial structures and, therefore, produce a signature pattern that allows us to distinguish three proteins.…”
Section: Resultsmentioning
confidence: 95%
“…Specifically, BSA shows seven characteristic peaks at 617, 650, 1219, 1355, 1499, 1522, and 1650 cm –1 , which could be attributed to C–C twisting, OH out-of-plane bending, the amine III of proteins, tryptophan, CC stretching in a benzenoid ring, carotene, and amide I, respectively. These peaks are almost missing in the case of LYS and OVA. Six peaks that were observed in SERS spectra of OVA are assigned to tryptophan, collagen, d­(CH), υs COO – (IgG), CC stretching in benzenoid ring, and protein amide I absorption from left to right, respectively. SERS features from LYS were also distinguishable from two other proteins. They are dominated by the bands of amino acids, such as the C–S stretching mode of cysteine, proline, phenylalanine, tyrosine, and amide I band of proteins, due to CO stretching (at 653, 825, 1032, 1164, and 1600 cm –1 , respectively). , These differences may be correlated with different amino acid species and protein spatial structures and, therefore, produce a signature pattern that allows us to distinguish three proteins.…”
Section: Resultsmentioning
confidence: 95%
“…Tracking the migration of various cells to different systems in vivo is essential to assess the effectiveness of immunotherapy. Zhang et al demonstrated the good performance of Au@PB-Gd @ovalbumin NPs (APG@OVA NPs), which enables PBs to coordinate core with gold nanoparticles in cyanide (CN) binding for dendritic cell (DC) activation and labeling [ 86 ]. The APG@OVA NPs agents could not only activate and label DCs, but also monitor DC movement in real time and accurately profile DC distribution in the lymphatic system.…”
Section: Application Of Enzyme Activity Of Pbnpsmentioning
confidence: 99%
“…Through the coating of ovalbumin (OVA) physically, APG@OVA NPs were provided. 47 First step: The Au NPs were prepared through the classic sodium citrate reduction process using sodium citrate and HAuCl 4 solutions. Second step: K 4 [Fe(CN) 6 ] and FeCl 3 were applied as the Prussian blue nanoparticles (PB) agent, which was reacted with GdCl 3 .…”
Section: Au–magnetic Organic Hybrid Core–shellsmentioning
confidence: 99%