甲啶铂与牛血清白蛋白相互作用的荧光光谱研究

用稳态荧光光谱及时间分辨荧光技术研究水溶液中甲啶铂与牛血清白蛋白(BSA)的相互作用。加入甲啶铂后,BSA荧光发射峰从335 nm红移到337.5 nm,并伴随着荧光强度的猝灭,表明甲啶铂与BSA发生了相互作用;单指数拟合得到的荧光寿命结果证实,甲啶铂对BSA的猝灭为静态猝灭;荧光寿命的双指数拟合结果表明,BSA的内在荧光主要是由第212位和第134位的色氨酸残基贡献的,BSA中第212位色氨酸残基和苯丙氨酸残基可能是甲啶铂的靶向目标。

Fluorescence Spectroscopy Study of the Interaction between Picoplatin and Bovine Serum Albumin

The interaction between picoplatin and bovine serum albumin (BSA) in aqueous solution was studied by steady-state fluorescence spectroscopy and time-resolved fluorescence techniques. With the introduction of picoplatin, the fluorescence emission peak of BSA redshifted from 335 nm to 337.5 nm, accompanied by the quenching of fluorescence intensity, indicating that there was interaction between picoplatin and BSA. The single exponential fitting of the fluorescence decay confirmed that the quenching of the BSA by picoplatin is static. The double exponential fitting of the fluorescence decay indicates that the intrinsic fluorescence of BSA is mainly contributed by the tryptophan (Trp) residues at the 212^th and 134^th positions. The 212^th Trp residue and the phenylalanine (Phe) residue in BSA may be the targets of picoplatin.