Wu Qihua, Zhu Manzhou, Guo Qingxiang. A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin[J]. Chinese Journal of Chemical Physics , 2004, 17(4): 476-480. doi: 10.1088/1674-0068/17/4/476-480
Citation: Wu Qihua, Zhu Manzhou, Guo Qingxiang. A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin[J]. Chinese Journal of Chemical Physics , 2004, 17(4): 476-480. doi: 10.1088/1674-0068/17/4/476-480

A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin

doi: 10.1088/1674-0068/17/4/476-480
Funds:  Project supported by the National Natural Science Foundation of China (20272057).This research was supported by the NSFC (No.20272057).
  • Received Date: 2003-05-05
  • Interactions of a series of dialkyl cationic lipids linking with bovine serum albumin (BSA) through acetal (linker) have been studied by the fluorescence spectroscopy. At low concentrations of cationic lipids, the fluorescence intensity of BSA decreased with binding of cationic lipid, and the maximum of emission wavelength shifted from (344±1)nm to (331±1)nm. It indicates that the BSA goes to uncoiled flexible conformation from its native structure. When the concentrations of lipids increased, the fluorescence intensity increased rapidly and then maintained unchanged. It reveals that two tryptophan residues of BSA are all enwrapped in the bilayer membrane, owing to the hydrophobic interactions between lipids and BSA.
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A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin

doi: 10.1088/1674-0068/17/4/476-480
Funds:  Project supported by the National Natural Science Foundation of China (20272057).This research was supported by the NSFC (No.20272057).

Abstract: Interactions of a series of dialkyl cationic lipids linking with bovine serum albumin (BSA) through acetal (linker) have been studied by the fluorescence spectroscopy. At low concentrations of cationic lipids, the fluorescence intensity of BSA decreased with binding of cationic lipid, and the maximum of emission wavelength shifted from (344±1)nm to (331±1)nm. It indicates that the BSA goes to uncoiled flexible conformation from its native structure. When the concentrations of lipids increased, the fluorescence intensity increased rapidly and then maintained unchanged. It reveals that two tryptophan residues of BSA are all enwrapped in the bilayer membrane, owing to the hydrophobic interactions between lipids and BSA.

Wu Qihua, Zhu Manzhou, Guo Qingxiang. A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin[J]. Chinese Journal of Chemical Physics , 2004, 17(4): 476-480. doi: 10.1088/1674-0068/17/4/476-480
Citation: Wu Qihua, Zhu Manzhou, Guo Qingxiang. A Fluorescence Study on the Interactions of Cationic Lipids with Bovine Serum Albumin[J]. Chinese Journal of Chemical Physics , 2004, 17(4): 476-480. doi: 10.1088/1674-0068/17/4/476-480

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