Biologically active halo-substituted ferrocenyl thioureas: synthesis, spectroscopic characterization, and DFT calculations

2018 ◽  
Vol 42 (9) ◽  
pp. 7154-7165 ◽  
Author(s):  
Faiza Asghar ◽  
Sadaf Rana ◽  
Saira Fatima ◽  
Amin Badshah ◽  
Bhajan Lal ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dft Calculations ◽  
Binding Affinity ◽  
Spectroscopic Characterization ◽  
Biologically Active ◽  
Dna Binding Affinity ◽  
Dna Binders

The DNA binding affinity of ferrocenyl complexes explored by CV and UV ascertain them as noble DNA binders. The computational measurements correlate well with the outcomes of electrochemistry and bio-activities.

Synthesis, spectroscopic investigation, and DFT study of N,N′-disubstituted ferrocene-based thiourea complexes as potent anticancer agents

2018 ◽  
Vol 47 (6) ◽  
pp. 1868-1878 ◽  
Author(s):  
Faiza Asghar ◽  
Saira Fatima ◽  
Sadaf Rana ◽  
Amin Badshah ◽  
Ian S. Butler ◽  
...  
Keyword(s):  
Dna Binding ◽  
Anticancer Activity ◽  
Binding Affinity ◽  
Anticancer Agents ◽  
Spectroscopic Investigation ◽  
Dft Study ◽  
Redox Potentials ◽  
Dna Binding Affinity ◽  
Dna Binders ◽  
Homo Lumo

The DNA binding affinity of ferrocenyl thioureas (A1–A9) explored by CV and UV ascertain them as noble DNA binders. The complexes also publicized decent antioxidant and anticancer activity. DFT-based HOMO/LUMO energies are comparable with experimentally calculated redox potentials.

5-Methyl-Benzofuro[3,2-b]quinoline Derivatives as DNA Binders

2013 ◽  
Vol 711 ◽  
pp. 73-78 ◽  
Author(s):  
Rui Fang Zhang ◽  
Rui Rui Zhang ◽  
Yu Jing Lu ◽  
Zhi Yun Du ◽  
Cheng Jie Fu ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Dna Binding ◽  
Binding Affinity ◽  
Binding Mode ◽  
Quinoline Derivatives ◽  
Lead Compound ◽  
Dna Binding Affinity ◽  
Intercalation Binding ◽  
Dna Binders ◽  
Derivatives Of

Several derivatives of 5-methyl-benzofuro [3,2-quinoline (O-isostere of cryptolepine) were synthesized. Spectrometric experiments and molecular modeling indicated that these derivatives interacted with duplex DNA by intercalation binding mode. The derivatives with aniline substituent exhibited superior DNA binding affinity to that of lead compound 5-methyl-benzofuro [3,2-quinoline.

Synthesis, Spectral Properties and DFT Calculations of new Ruthenium (II) Polypyridyl Complexes; DNA Binding Affinity and in Vitro Cytotoxicity Activity

2017 ◽  
Vol 27 (4) ◽  
pp. 1513-1530 ◽  
Author(s):  
Rajender Reddy Mallepally ◽  
Nagamani Chintakuntla ◽  
Venkat Reddy Putta ◽  
Nagasuryaprasad K ◽  
Ravi Kumar Vuradi ◽  
...  
Keyword(s):  
Dna Binding ◽  
Dft Calculations ◽  
Binding Affinity ◽  
Spectral Properties ◽  
In Vitro Cytotoxicity ◽  
Polypyridyl Complexes ◽  
Cytotoxicity Activity ◽  
Dna Binding Affinity

scholarly journals Lowering DNA binding affinity of SssI DNA methyltransferase does not enhance the specificity of targeted DNA methylation in E. coli

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Krystyna Ślaska-Kiss ◽  
Nikolett Zsibrita ◽  
Mihály Koncz ◽  
Pál Albert ◽  
Ákos Csábrádi ◽  
...  
Keyword(s):  
Dna Methylation ◽  
Dna Binding ◽  
Binding Affinity ◽  
Dna Methyltransferase ◽  
Restriction Enzymes ◽  
Dna Binding Protein ◽  
E Coli ◽  
Dna Binding Affinity ◽  
Higher Eukaryotes

AbstractTargeted DNA methylation is a technique that aims to methylate cytosines in selected genomic loci. In the most widely used approach a CG-specific DNA methyltransferase (MTase) is fused to a sequence specific DNA binding protein, which binds in the vicinity of the targeted CG site(s). Although the technique has high potential for studying the role of DNA methylation in higher eukaryotes, its usefulness is hampered by insufficient methylation specificity. One of the approaches proposed to suppress methylation at unwanted sites is to use MTase variants with reduced DNA binding affinity. In this work we investigated how methylation specificity of chimeric MTases containing variants of the CG-specific prokaryotic MTase M.SssI fused to zinc finger or dCas9 targeting domains is influenced by mutations affecting catalytic activity and/or DNA binding affinity of the MTase domain. Specificity of targeted DNA methylation was assayed in E. coli harboring a plasmid with the target site. Digestions of the isolated plasmids with methylation sensitive restriction enzymes revealed that specificity of targeted DNA methylation was dependent on the activity but not on the DNA binding affinity of the MTase. These results have implications for the design of strategies of targeted DNA methylation.

scholarly journals Quantification of transcription factor-DNA binding affinity in a living cell

2015 ◽  
Vol 44 (7) ◽  
pp. 3045-3058 ◽  
Author(s):  
Sergey Belikov ◽  
Otto G. Berg ◽  
Örjan Wrange
Keyword(s):  
Transcription Factor ◽  
Dna Binding ◽  
Binding Affinity ◽  
Living Cell ◽  
Dna Binding Affinity
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