2.50
Hdl Handle:
http://hdl.handle.net/10033/196972
Title:
Synthesis and characterization of human transferrin-stabilized gold nanoclusters.
Authors:
Le Guével, Xavier; Daum, Nicole; Schneider, Marc
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.
Affiliation:
Pharmaceutical Nanotechnology, Saarland University, Saarbrücken, Germany.
Citation:
Synthesis and characterization of human transferrin-stabilized gold nanoclusters. 2011, 22 (27):275103 Nanotechnology
Journal:
Nanotechnology
Issue Date:
8-Jul-2011
URI:
http://hdl.handle.net/10033/196972
DOI:
10.1088/0957-4484/22/27/275103
PubMed ID:
21613679
Type:
Article
Language:
en
ISSN:
1361-6528
Appears in Collections:
publications of the division Wirkstoff-Transport (DDEL)

Full metadata record

DC FieldValue Language
dc.contributor.authorLe Guével, Xavieren
dc.contributor.authorDaum, Nicoleen
dc.contributor.authorSchneider, Marcen
dc.date.accessioned2011-12-13T13:53:35Z-
dc.date.available2011-12-13T13:53:35Z-
dc.date.issued2011-07-08-
dc.identifier.citationSynthesis and characterization of human transferrin-stabilized gold nanoclusters. 2011, 22 (27):275103 Nanotechnologyen
dc.identifier.issn1361-6528-
dc.identifier.pmid21613679-
dc.identifier.doi10.1088/0957-4484/22/27/275103-
dc.identifier.urihttp://hdl.handle.net/10033/196972-
dc.description.abstractHuman 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.en
dc.language.isoenen
dc.titleSynthesis and characterization of human transferrin-stabilized gold nanoclusters.en
dc.typeArticleen
dc.contributor.departmentPharmaceutical Nanotechnology, Saarland University, Saarbrücken, Germany.en
dc.identifier.journalNanotechnologyen

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