Loading...
Synthesis and characterization of human transferrin-stabilized gold nanoclusters.
Le Guével, Xavier Daum, Nicole Schneider, Marc
Le Guével, Xavier
Daum, Nicole
Schneider, Marc
Citations
Altmetric:
Advisors
Editors
Other Contributors
Issue Date
2011-07-08
Submitted date
Files
Loading...
original manuscript
Adobe PDF, 3.31 MB
Loading...
supporting information
Adobe PDF, 2.4 MB
Other Titles
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.
Citation
Synthesis and characterization of human transferrin-stabilized gold nanoclusters. 2011, 22 (27):275103 Nanotechnology
Publisher
Journal
PubMed ID
PubMed Central ID
Additional Links
Embedded video
Type
Article
Language
en
Description
Series/Report no.
ISSN
1361-6528