Journal
LUMINESCENCE
Volume 30, Issue 8, Pages 1176-1183Publisher
WILEY-BLACKWELL
DOI: 10.1002/bio.2873
Keywords
transferrin; cyanine dye; fluorescent quenching; conformational transition; docking
Categories
Funding
- National Natural Science Foundation of China [21443011]
- Hebei Province Nature Science Foundation of China [B2012401026]
- Hebei Education Department of China [2011106]
- open project program of Beijing National Laboratory for Molecular Sciences
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Complexation between the primary carrier of ligands in blood plasma, human serum transferrin (Tf), and a cyanine dye, 3,3'-di(3-sulfopropyl)-4,5,4', 5'-dibenzo-9-phenyl-thiacarbocyanine-triethylam monium salt (PTC) was investigated using fluorescence spectra, UV/Vis absorption spectra, synchronous fluorescence spectra, circular dichroism (CD) and molecular dynamic docking. The experimental results demonstrate that the formation of PTC-Tf complex is stabilized by van der Waal's interactions and hydrogen bonds, and the binding constants were found to be 8.55 x 10(6), 8.19 x 10(6) and 1.75 x 10(4) M-1. Moreover, fluorescence experiments prove that the operational mechanism for the fluorescence quenching is static quenching and non-radiative energy transfer. Structural investigation of the PTC-Tf complexes via synchronous fluorescence spectra and CD showed that the structure of Tf became more stable with a major increase in the a-helix content and increased polarity around the tryptophan residues after PTC binding. In addition, molecular modeling highlights the residues located in the N-lobe, which retain high affinity for PTC. The mode of action of the PTC-Tf complex is illustrated by these results, and may provide an effective pathway for the transport and targeted delivery of antitumor agents. Copyright (C) 2015 John Wiley & Sons, Ltd.
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