Time-Resolved Fluorescence Anisotropy Study of the Interaction Between DNA and a Peptide Truncated from the p53 Protein Core Domain

被引：3

作者：

Liu, Chengxuan ^{[1
]}

Liang, Gaiting ^{[1
]}

Liu, Zhen ^{[1
]}

Zu, Lily ^{[1
]}

机构：

[1] Beijing Normal Univ, Coll Chem, Beijing 100875, Peoples R China

来源：

JOURNAL OF FLUORESCENCE | 2014年 / 24卷 / 02期

基金：

中国国家自然科学基金;

关键词：

Fluorescence spectroscopy; Time-resolved anisotropy; Interaction between peptide andDNA; Specific recognition; RESONANCE ENERGY-TRANSFER; CRYSTAL-STRUCTURE; COOPERATIVE BINDING; TETRAMERIC P53; RECOGNITION; MUTATIONS; CONTAINS; DYNAMICS; APTAMER; REGIONS;

D O I：

10.1007/s10895-013-1322-7

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Time-resolved fluorescence anisotropy spectroscopy was applied to study the interaction between a peptide truncated from the binding site of tumor suppressor p53 protein and the DNAs covalently labeled with 6-carboxyfluorescein (FAM) dye. Fluorescence intensity quenching and changes of anisotropy decay lifetime were monitored when FAM labeled DNA formed complex with the peptide. The results demonstrated that the sequence of DNA could not define the binding specificity between the peptide and DNA. But the anisotropy decay of FAM can be used to examine the binding affinity of the peptide to DNA. The fluorescent dynamics of FAM can also be used to represent the rigidity of the complex formed between the peptide and DNA.

引用

页码：533 / 539

页数：7