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	磷脂酰胆碱与牛血清白蛋白相互作用的FT-IR研究; FT-IR study of the interaction between phosphatidylcholine and bovine serum albumin
	王凡 ; 杨展澜 ; 张莉 ; 翁诗甫 ; 吴瑾光
	2004
关键词	FT-IR FT-Raman FT-IR FT-Raman phosphatidylcholine BSA 磷脂酰胆碱(PC) 牛血清白蛋白(BSA)
英文摘要	利用傅立叶变换红外(FT-IR)和拉曼(FT-Raman)光谱研究了高浓度磷脂酰胆碱(PC)与牛血清白蛋白(BSA)的相互作用,及Eu3+对该作用的影响.FT-IR结果显示,PC/BSA混合体系中二者的相互作用主要发生在PC头部极性基团,且这一作用随BSA含量的增加而增强,作用后蛋白质二级结构中α螺旋的比例有所增加.FT-Raman光谱说明PC与BSA的相互作用影响磷脂CH链的排列有序程度.PC/BSA/Eu3+体系的红外光谱显示,Eu3+与PC的磷氧键发生了强相互作用,并使蛋白α螺旋的比例进一步增加.; The interactions between phosphatidylcholine (PC) and bovine serum albumin (BSA) were studied by FT-IR and FT-Raman spectroscopies, then the influence of lanthanide ion Eu3+ on the PC/BSA mixture system was discussed. In the region of 900 similar to 1300 cm(-1), FT-IR spectra showed that the bands of P = O, P-O-C and C - 0 of the PC/BSA mixture were shifted compared with the corresponding bands of pure PC and BSA, and the more content of BSA (relative to the content of PC) the greater shift was observed. The curve-fitting result of amide I band indicated that an increase of alpha-helix fragments in the PC/BSA mixture. Fr-Raman spectra showed that the CH stretching bands in the PC/BSA mixture were varied, which indicated a disturbance of PC's long chains in the mixture system. After Eu ion was added into the PC/BSA system, the P = 0 stretching vibration bands in FT-IR spectra shifted from 1241 to 1208 cm(-1). This helped us to conclude that the Eu ions bind to the P = 0 group in the PC/BSA mixture.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000224795800004&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; SCI(E); 中文核心期刊要目总览(PKU); 中国科技核心期刊(ISTIC); 中国科学引文数据库(CSCD); 2; 10; 1186-1190; 20
语种	中文
出处	万方 ; 知网 ; SCI
出版者	物理化学学报
内容类型	其他
源URL	[http://hdl.handle.net/20.500.11897/80111]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	王凡,杨展澜,张莉,等. 磷脂酰胆碱与牛血清白蛋白相互作用的FT-IR研究, FT-IR study of the interaction between phosphatidylcholine and bovine serum albumin. 2004-01-01.

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