Abstract |
Purpure-18-imide was synthesized based on the porphyrin's special affinity for cancer cells and the antitumor activity of pyrrolidine compound. The binding reaction between purpure-18-imide and bovine serum albumins (BSA) in aqueous was studied by fluorescence and UV-Vis absorption spectra. The research results indicated that the combination reaction of them was a single static quenching process. In aqueous, purpure-18-imide strongly bound BSA with molar ratio of 1:1. The binding constant K0 was 5.386 x 10(5) L x mol(-1). The shortest binding distance (r = 3.54 nm) and energy transfer efficiencies (E = 0.26) between donor (BSA) and acceptor (purpure-18-imide) were obtained by Forster's nonradiative energy transfer mechanism.
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Authors | Jin-jun Wang, Yong-ming Liu, Li Li |
Journal | Guang pu xue yu guang pu fen xi = Guang pu
(Guang Pu Xue Yu Guang Pu Fen Xi)
Vol. 25
Issue 4
Pg. 594-7
(Apr 2005)
ISSN: 1000-0593 [Print] China |
PMID | 16097695
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Imides
- Porphyrins
- purpure-18-imide
- purpurin 18
- Serum Albumin, Bovine
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Topics |
- Algorithms
- Animals
- Cattle
- Energy Transfer
- Fluorescence
- Imides
(chemical synthesis, chemistry, metabolism)
- Kinetics
- Models, Chemical
- Molecular Structure
- Porphyrins
(chemical synthesis, chemistry)
- Protein Binding
- Serum Albumin, Bovine
(chemistry, metabolism)
- Spectrometry, Fluorescence
- Spectrophotometry
- Spectrophotometry, Ultraviolet
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