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合成系列含缩醛的双链正离子类脂分子 ,并用荧光光谱研究其与牛血清蛋白 (BSA)的相互作用 .通过荧光的变化 ,解释蛋白质构象的变化 .在低类脂浓度时 ,少量类脂分子束缚在牛血清蛋白周围 ,荧光有很大幅度的淬灭 ,蛋白质本身肽链被解开 ,与此同时最大发射波长从 (3 44± 1)nm蓝移到 (3 3 1± 1)nm .由于疏水相互作用 ,更多类脂分子不断地聚集在蛋白质周围 ,牛血清蛋白中的两个色氨酸残基被完全地包裹在类脂分子形成的双分子膜中 ,荧光强度不断增加直到恒定不变
A series of acetal double-stranded cationic lipids were synthesized and their interaction with bovine serum albumin (BSA) was studied by fluorescence spectroscopy.The changes of protein conformations were explained by the change of fluorescence.When the concentration of lipids was low, The lipid molecules are bound around the bovine serum albumin, the fluorescence is greatly quenched, and the peptide chain of the protein itself is released. At the same time, the maximum emission wavelength shifts from (3 44 ± 1) nm blue to (3 3 1 ± 1) nm. Due to the hydrophobic interaction, more lipid molecules accumulate continuously around the protein. The two tryptophan residues in the bovine serum albumin are completely encapsulated in the bilayer membrane formed by the lipid molecules and the fluorescence intensity is continuously increased Until constant