scholarly journals Synthesis Characterization and DNA Interaction Studies of a New Zn(II) Complex Containing Different Dinitrogen Aromatic Ligands

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Nahid Shahabadi ◽  
Somaye Mohammadi
Keyword(s):  
Cyclic Voltammetry ◽  
Binding Sites ◽  
Dna Interaction ◽  
Mononuclear Complex ◽  
Cd Spectra ◽  
Base Pairs ◽  
Binding Properties ◽  
Analysis Techniques ◽  
Ft Ir ◽  
Dna Binding Properties

A mononuclear complex of Zn(II), [Zn(DIP)2(DMP)] (NO3)2·2H2O in which DIP is 4,7-diphenyl-1,10-phenanthroline and DMP is 4,4′-dimethyl-2,2′-bipyridine has been prepared and characterized by1HNMR spectroscopy, FT-IR, UV-Vis and elemental analysis techniques. DNA-binding properties of the complex were studied using UV-vis spectra, circular dichroism (CD) spectra, fluorescence, cyclic voltammetry (CV), and viscosity measurements. The results indicate that this zinc(II) complex can intercalate into the stacked base pairs of DNA and compete with the strong intercalator ethidium bromide for the intercalative binding sites.

scholarly journals Synthesis, Characterization, DNA Binding, and Photocleavage Activity of Oxorhenium (V) Complexes withα-Diimine and Quinoxaline Ligands

2010 ◽  
Vol 2010 ◽  
pp. 1-9 ◽  
Author(s):  
Christiana A. Mitsopoulou ◽  
Constantinos Dagas
Keyword(s):  
Cyclic Voltammetry ◽  
Dna Binding ◽  
Dna Cleavage ◽  
2D Nmr ◽  
Base Pairs ◽  
Binding Properties ◽  
Supercoiled Form ◽  
Dna Base ◽  
Dna Base Pairs ◽  
Dna Binding Properties

The complex [ReOCl3pq] (1) (where pq = 2-(2′pyridyl)quinoxaline) has been synthesized and fully characterized by UV-Vis, FTIR, 1 and 2D NMR, and cyclic voltammetry (CV). The DNA-binding properties of the complex1as well as of the compounds [ReOCl3bpy] (2), [ReOCl3phen] (3), and pq (4) were investigated by UV-spectrophotometric (melting curves), CV (cyclic voltammetry), and viscosity measurements. Experimental data suggest that complex1intercalates into the DNA base pairs. Upon irradiation, complex1was found to promote the cleavage of plasmid pBR 322 DNA from supercoiled form I to nicked form II. The mechanism of the DNA cleavage by complex1was also investigated.

scholarly journals Structural characterization and DNA-binding properties of Sm(III) complex with ofloxacin using spectroscopic methods

2009 ◽  
Vol 23 (2) ◽  
pp. 103-111 ◽  
Author(s):  
Changyun Chen ◽  
Kai Chen ◽  
Qi Long ◽  
Meihua Ma ◽  
Fei Ding
Keyword(s):  
Binding Sites ◽  
Nmr Spectra ◽  
Uv Spectroscopy ◽  
Binding Constants ◽  
Binding Properties ◽  
H Nmr ◽  
Elemental Analyses ◽  
Displacement Experiments ◽  
Ct Dna ◽  
Dna Binding Properties

A novel complex Sm(III) complex with ofloxacin was synthesized and characterized on the basis of elemental analyses, molar conductivities, IR spectra, thermal analysis (TG-DSC),1H-NMR spectra. Then, spectrometric titration, ethdium bromide displacement experiments by UV spectroscopy, ionic influence, viscosity measurements and Circular Dichroism (CD) spectroscopic measurements were conducted to characterize the interaction between the complex and CT-DNA. Results obtained indicate that the complex bound with CT-DNA via an intercalation mechanism. The binding constants and binding sites number of the Sm(III) complex with CT-DNA were 1.80×105l·mol−1and 1, respectively.

Structure, cyclic voltammetry and DNA-binding properties of the bis(pyridine)bis(sparfloxacinato)nickel(II) complex

Polyhedron ◽  
2009 ◽  
Vol 28 (15) ◽  
pp. 3265-3271 ◽  
Author(s):  
Kalliopi C. Skyrianou ◽  
Catherine P. Raptopoulou ◽  
Vassilis Psycharis ◽  
Dimitris P. Kessissoglou ◽  
George Psomas
Keyword(s):  
Cyclic Voltammetry ◽  
Dna Binding ◽  
Binding Properties ◽  
Dna Binding Properties

The Arabidopsis class I TCP transcription factor AtTCP11 is a developmental regulator with distinct DNA-binding properties due to the presence of a threonine residue at position 15 of the TCP domain

2011 ◽  
Vol 435 (1) ◽  
pp. 143-155 ◽  
Author(s):  
Ivana L. Viola ◽  
Nora G. Uberti Manassero ◽  
Rodrigo Ripoll ◽  
Daniel H. Gonzalez
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Class I ◽  
Binding Properties ◽  
Threonine Residue ◽  
Dna Binding Specificity ◽  
Systematic Evolution ◽  
Enrichment Experiments ◽  
Exponential Enrichment ◽  
Dna Binding Properties

The TCP domain is a DNA-binding domain present in plant transcription factors that modulate different processes. In the present study, we show that Arabidopsis class I TCP proteins are able to interact with a dyad-symmetric sequence composed of two GTGGG half-sites. TCP20 establishes symmetric interactions with the 5′ half of each strand, whereas TCP11 interacts mainly with the 3′ half. SELEX (systematic evolution of ligands by exponential enrichment) experiments with TCP15 and TCP20 indicated that these proteins have similar, although not identical, DNA-binding preferences and are able to interact with non-palindromic binding sites of the type GTGGGNCCNN. TCP11 shows a different DNA-binding specificity, with a preference for the sequence GTGGGCCNNN. The distinct DNA-binding properties of TCP11 are due to the presence of a threonine residue at position 15 of the TCP domain, a position that is occupied by an arginine residue in most TCP proteins. TCP11 also forms heterodimers with TCP15 that have increased DNA-binding efficiency. The expression in plants of a repressor form of TCP11 demonstrated that this protein is a developmental regulator that influences the growth of leaves, stems and petioles, and pollen development. The results suggest that changes in DNA-binding preferences may be one of the mechanisms through which class I TCP proteins achieve functional specificity.

scholarly journals DNA-binding activities of the Drosophila melanogaster even-skipped protein are mediated by its homeo domain and influenced by protein context.

1988 ◽  
Vol 8 (11) ◽  
pp. 4598-4607 ◽  
Author(s):  
T Hoey ◽  
R Warrior ◽  
J Manak ◽  
M Levine
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Consensus Sequence ◽  
Binding Properties ◽  
Binding Behavior ◽  
High Affinity ◽  
Homeo Box ◽  
Acid Protein ◽  
Dna Binding Properties ◽  
Amino Acid Protein

The homeo box gene even-skipped (eve) encodes a 376-amino-acid protein that binds with high affinity to sequences located near the 5' termini of the eve and en genes. The 5' en sites are A + T rich and contain copies of the 10-base-pair (bp) consensus sequence T-C-A-A-T-T-A-A-A-T. In contrast, the 5' eve sites are G + C rich and contain the 9-bp sequence T-C-A-G-C-A-C-C-G. Among the five different homeo box proteins that have been tested for binding, eve is unique in that it shows virtually equal preference for the A + T-rich 5' en binding sites and the G + C-rich 5' eve sites. Most of the other proteins bind with a relatively higher affinity to the en sites than to the eve sites. In an effort to identify the regions of the eve protein that are responsible for its efficient binding to both classes of recognition sequences, we analyzed the DNA-binding properties of various mutant eve proteins. These studies suggest that the homeo domain of the eve protein is responsible for both binding activities. However, mutations in distant regions of the protein influenced the binding behavior of the eve homeo domain and caused a reduction in binding to the G + C class of recognition sites. We propose that the protein context of the homeo domain can influence its DNA-binding properties.

scholarly journals Synthesis, Cytotoxic Activity, and DNA Binding Properties of Copper (II) Complexes with Hesperetin, Naringenin, and Apigenin

2009 ◽  
Vol 2009 ◽  
pp. 1-9 ◽  
Author(s):  
Mingxiong Tan ◽  
Jinchan Zhu ◽  
Yingming Pan ◽  
Zhenfeng Chen ◽  
Hong Liang ◽  
...  
Keyword(s):  
Cell Lines ◽  
Human Cancer ◽  
Free Ligand ◽  
Binding Properties ◽  
Human Cancer Cell Lines ◽  
Calf Thymus ◽  
Ft Ir ◽  
Hepg2 Cell Lines ◽  
Dna Binding Properties

Complexes of copper (II) with hesperetin, naringenin, and apigenin of general composition[CuL2(H2O)2]⋅nH2O(1–3) have been synthesized and characterized by elemental analysis, UV-Vis, FT-IR, ESI-MS, and TG-DTG thermal analysis. The free ligands and the metal complexes have been tested in vitro against human cancer cell lines hepatocellular carcinoma (HepG-2), gastric carcinomas (SGC-7901), and cervical carcinoma (HeLa). Complexes1and3were found to exhibit growth inhibition of SGC-7901 and HepG2 cell lines with respect to the free ligands; the inhibitory rate of complex1is 43.2% and 43.8%, while complex 3 is 46% and 36%, respectively. The interactions of complex1and its ligand Hsp with calf thymus DNA were investigated by UV-Vis, fluorescence, and CD spectra. Both complex1and Hsp were found to bind DNA in intercalation modes, and the binding affinity of complex1was stronger than that of free ligand.

DNA-binding activities of the Drosophila melanogaster even-skipped protein are mediated by its homeo domain and influenced by protein context

1988 ◽  
Vol 8 (11) ◽  
pp. 4598-4607
Author(s):  
T Hoey ◽  
R Warrior ◽  
J Manak ◽  
M Levine
Keyword(s):  
Dna Binding ◽  
Binding Sites ◽  
Consensus Sequence ◽  
Binding Properties ◽  
Binding Behavior ◽  
High Affinity ◽  
Homeo Box ◽  
Acid Protein ◽  
Dna Binding Properties ◽  
Amino Acid Protein

The homeo box gene even-skipped (eve) encodes a 376-amino-acid protein that binds with high affinity to sequences located near the 5' termini of the eve and en genes. The 5' en sites are A + T rich and contain copies of the 10-base-pair (bp) consensus sequence T-C-A-A-T-T-A-A-A-T. In contrast, the 5' eve sites are G + C rich and contain the 9-bp sequence T-C-A-G-C-A-C-C-G. Among the five different homeo box proteins that have been tested for binding, eve is unique in that it shows virtually equal preference for the A + T-rich 5' en binding sites and the G + C-rich 5' eve sites. Most of the other proteins bind with a relatively higher affinity to the en sites than to the eve sites. In an effort to identify the regions of the eve protein that are responsible for its efficient binding to both classes of recognition sequences, we analyzed the DNA-binding properties of various mutant eve proteins. These studies suggest that the homeo domain of the eve protein is responsible for both binding activities. However, mutations in distant regions of the protein influenced the binding behavior of the eve homeo domain and caused a reduction in binding to the G + C class of recognition sites. We propose that the protein context of the homeo domain can influence its DNA-binding properties.

scholarly journals Differential DNA Binding of Transcriptional Regulator PcaU from Acinetobacter sp. Strain ADP1

2002 ◽  
Vol 184 (7) ◽  
pp. 1988-1997 ◽  
Author(s):  
Roland Popp ◽  
Tobias Kohl ◽  
Patricia Patz ◽  
Gaby Trautwein ◽  
Ulrike Gerischer
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Binding Sites ◽  
Specific Binding ◽  
Transcriptional Regulator ◽  
Intrinsic Curvature ◽  
Binding Properties ◽  
Expression Of Genes ◽  
Intergenic Dna ◽  
Dna Binding Properties

ABSTRACT Transcriptional regulator PcaU from Acinetobacter sp. strain ADP1 governs expression of genes for protocatechuate degradation (pca genes) as a repressor or an activator depending on the levels of the inducer protocatechuate and of its own gene. PcaU is a member of the IclR protein family. Here the DNA binding properties of the purified protein are described in terms of the location of the binding sites and the affinity to these sites. Native PcaU was purified after overexpression of the pcaU gene in Escherichia coli. It is a dimer in solution. The binding site in the pcaU-pcaI intergenic region is located between the two divergent promoters covering 45 bp, which includes three perfect 10-bp repetitions. A PcaU binding site downstream of pcaU is covered by PcaU across two palindromic sequence repetitions. The affinity of PcaU for the intergenic binding sites is 50-fold higher (dissociation constant [Kd ], 0.16 nM) than the affinity for the site downstream of pcaU (Kd , 8 nM). The binding of PcaU was tested after modifications of the intergenic binding site. Removal of any external sequence repetition still allowed for specific binding of PcaU, but the affinity was significantly reduced, suggesting an important role for all three sequence repetitions in gene expression. The involvement of DNA bending in the regulatory process is suggested by the observed strong intrinsic curvature displayed by the pcaU-pcaI intergenic DNA.

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