林产化学与工业2017，Vol.37Issue(5)：79-87,9.DOI:10.3969/j.issn.0253-2417.2017.05.010
金属离子对花椒毒酚结合牛血清白蛋白体系的影响
Interactions Between Drugs and Bovine Serum Albumin in the Presence of Metal Ions by Spectral Methods
摘要
Abstract
The mechanisms of the interaction between xanthotoxol ( XAL) and bovine serum albumin ( BSA) were investigated by fluorescence and circular dichroism (CD) spectrometry, as well as the effects of common metal ions (Fe3+, Cu2+, Zn2+, Cr3+) on the XAL-BSA binding.The quenching constants (kq) calculated by Stern-Volmer equation under 290,297 and 304 K were 6.316 ×1013 ,4.402 ×1013 and 3.554 ×1013 L/(mol· s), respectively.The result indicated that XAL could quench the intrinsic fluorescence of BSA strongly , and the quenching mechanism was static quenching process .The binding constant ( K) of XAL to BSA at 297 K was 3.47 ×105 L/mol.The addition of metal ions changed the binding constant .The distance between the tryptophan residues in BSA and XAL was 5.29 nm by using F?ster's equation, and it decreased after interaction with metal ions . The CD spectrometry demonstrated that the secondary structure of BSA changed after its interaction with XAL , and α-helix content decreased; the secondary structure of BSA was also changed by addition of metal ions and α-helix content furtherreduced .关键词
花椒毒酚/牛血清白蛋白/相互作用Key words
xanthotoxol/bovine serum albumin/interaction分类
化学化工引用本文复制引用
曹洪坤,金晓伟,张恩风,于慧,石婧楠,边贺东..金属离子对花椒毒酚结合牛血清白蛋白体系的影响[J].林产化学与工业,2017,37(5):79-87,9.基金项目
国家自然科学基金资助项目(21061002, 21361003, 21101035) （21061002, 21361003, 21101035）
