title: Time-Resolved Fluorescence Anisotropy Study of the Interaction Between DNA and a Peptide Truncated from the p53 Protein Core Domain.
abstract: 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.
authors.affiliation: College of Chemistry, Beijing Normal University, Beijing, 100875, Peoples Republic of China.
authors.forename: Chengxuan
authors.initials: C
authors.lastname: Liu
authors.affiliation: College of Chemistry, Beijing Normal University, Beijing, 100875, Peoples Republic of China.
authors.forename: Gaiting
authors.initials: G
authors.lastname: Liang
authors.affiliation: College of Chemistry, Beijing Normal University, Beijing, 100875, Peoples Republic of China.
authors.forename: Zhen
authors.initials: Z
authors.lastname: Liu
authors.affiliation: College of Chemistry, Beijing Normal University, Beijing, 100875, Peoples Republic of China. zull@bnu.edu.cn.
authors.forename: Lily
authors.initials: L
authors.lastname: Zu
mesh_terms: D004247:DNA / Q000737:chemistry*; D005454:Fluorescence Polarization; D006801:Humans; D010455:Peptides / Q000737:chemistry*; D000072417:Protein Domains; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry*
chemical_list: D010455:Peptides; D016159:Tumor Suppressor Protein p53; D004247:DNA
keywords: Fluorescence spectroscopy; Interaction between peptide and DNA; Specific recognition; Time-resolved anisotropy