請用此 Handle URI 來引用此文件: http://hdl.handle.net/11455/34482
標題: Is association of labile enediyne chromophore a mutually assured protection for carrier protein?
作者: Kandaswamy, J.
金德航
Hariharan, P.
Kumar, T.K.S.
Yu, C.
Lu, T.J.
Chin, D.H.
陸大榮
關鍵字: enediyne
neocarzinostatin
chromophore
ligand binding
holoprotein
protein stability
apo-neocarzinostatin
crystal-structure
escherichia-coli
binding
apoprotein
aponeocarzinostatin
stabilization
denaturation
assignment
mechanism
期刊/報告no:: Analytical Biochemistry, Volume 381, Issue 1, Page(s) 18-26.
摘要: Most conjugate proteins undergo both conformational and stability changes on ligand removal. When architecture remains unchanged in the Protein holo and apo forms, it is uncertain whether the protein stability also remains unaltered in both of the forms. Neocarzinostatin (NCS), a chromoprotein possessing a potent enediyne chromophore stands for such an instance. Protein-chromophore interaction has not been thoroughly explored previously due to a lack of strategies to independently and simultaneously monitor changes in the NCS conjugates. Here we report a method by which one can detect the signal exclusively from only one of the NCS conjugates without the spectral interference from the other. Stability of the NCS protein is significantly correlated to the protein-bound chromophore, irrespective of denaturation by heat, pH, Urea, or ethanol. Despite the similarity in protein backbone conformation, protein stability of the NCS holo form diminishes and equalizes to that of the apo form when the chromophore is released and degraded. Although the enediyne chromophore is highly unstable, it intriguingly protects the protein by which it is protected. Significant mutual reliance between the carrier protein and its naturally associated ligand unveils important information on the NCS drug stability. (c) 2008 Elsevier Inc. All rights reserved.
URI: http://hdl.handle.net/11455/34482
ISSN: 0003-2697
文章連結: http://dx.doi.org/10.1016/j.ab.2008.06.017
顯示於類別:化學系所

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