Synthesis and characterization of human transferrin-stabilized gold nanoclusters.
dc.contributor.author | Le Guével, Xavier | |
dc.contributor.author | Daum, Nicole | |
dc.contributor.author | Schneider, Marc | |
dc.date.accessioned | 2011-12-13T13:53:35Z | en |
dc.date.available | 2011-12-13T13:53:35Z | en |
dc.date.issued | 2011-07-08 | en |
dc.identifier.citation | Synthesis and characterization of human transferrin-stabilized gold nanoclusters. 2011, 22 (27):275103 Nanotechnology | en |
dc.identifier.issn | 1361-6528 | en |
dc.identifier.pmid | 21613679 | en |
dc.identifier.doi | 10.1088/0957-4484/22/27/275103 | en |
dc.identifier.uri | http://hdl.handle.net/10033/196972 | en |
dc.description.abstract | Human transferrin has been biolabelled with gold nanoclusters (Au NCs) using a simple, fast and non-toxic method. These nanocrystals (<2 nm) are stabilized in the protein via sulfur groups and have a high fluorescence emission in the near infrared region (QY=4.3%; λem=695 nm). Structural investigation and photophysical measurements show a high population of clusters formed of 22-33 gold atoms covalently bound to the transferrin. In solutions with pH ranging from 5 to 10 and in buffer solutions (PBS, HEPES), those biolabelled proteins exhibit a good stability. No significant quenching effect of the fluorescent transferrin has been detected after iron loading of iron-free transferrin (apoTf) and in the presence of a specific polyclonal antibody. Additionally, antibody-induced agglomeration demonstrates no alteration in the protein activity and the receptor target ability. MTT and Vialight® Plus tests show no cytotoxicity of these labelled proteins in cells (1 µg ml(-1)-1 mg ml(-1)). Cell line experiments (A549) indicate also an uptake of the iron loaded fluorescent proteins inside cells. These remarkable data highlight the potential of a new type of non-toxic fluorescent transferrin for imaging and targeting. | |
dc.language.iso | en | en |
dc.title | Synthesis and characterization of human transferrin-stabilized gold nanoclusters. | en |
dc.type | Article | en |
dc.contributor.department | Pharmaceutical Nanotechnology, Saarland University, Saarbrücken, Germany. | en |
dc.identifier.journal | Nanotechnology | en |
refterms.dateFOA | 2018-06-12T18:05:51Z | |
html.description.abstract | Human transferrin has been biolabelled with gold nanoclusters (Au NCs) using a simple, fast and non-toxic method. These nanocrystals (<2 nm) are stabilized in the protein via sulfur groups and have a high fluorescence emission in the near infrared region (QY=4.3%; λem=695 nm). Structural investigation and photophysical measurements show a high population of clusters formed of 22-33 gold atoms covalently bound to the transferrin. In solutions with pH ranging from 5 to 10 and in buffer solutions (PBS, HEPES), those biolabelled proteins exhibit a good stability. No significant quenching effect of the fluorescent transferrin has been detected after iron loading of iron-free transferrin (apoTf) and in the presence of a specific polyclonal antibody. Additionally, antibody-induced agglomeration demonstrates no alteration in the protein activity and the receptor target ability. MTT and Vialight® Plus tests show no cytotoxicity of these labelled proteins in cells (1 µg ml(-1)-1 mg ml(-1)). Cell line experiments (A549) indicate also an uptake of the iron loaded fluorescent proteins inside cells. These remarkable data highlight the potential of a new type of non-toxic fluorescent transferrin for imaging and targeting. |