DNA Groove Binding

2020 ◽  
Author(s):  
Keyword(s):  
1993 ◽  
Vol 268 (6) ◽  
pp. 3944-3951
Author(s):  
E. Trotta ◽  
E. D'Ambrosio ◽  
N. Del Grosso ◽  
G. Ravagnan ◽  
M. Cirilli ◽  
...  

2021 ◽  
Vol 14 (7) ◽  
pp. 685
Author(s):  
Sandra Amanda Kozieł ◽  
Monika Katarzyna Lesiów ◽  
Daria Wojtala ◽  
Edyta Dyguda-Kazimierowicz ◽  
Dariusz Bieńko ◽  
...  

A group of cytotoxic half-sandwich iridium(III) complexes with aminomethyl(diphenyl)phosphine derived from fluoroquinolone antibiotics exhibit the ability to (i) accumulate in the nucleus, (ii) induce apoptosis, (iii) activate caspase-3/7 activity, (iv) induce the changes in cell cycle leading to G2/M phase arrest, and (v) radicals generation. Herein, to elucidate the cytotoxic effects, we investigated the interaction of these complexes with DNA and serum proteins by gel electrophoresis, fluorescence spectroscopy, circular dichroism, and molecular docking studies. DNA binding experiments established that the complexes interact with DNA by moderate intercalation and predominance of minor groove binding without the capability to cause a double-strand cleavage. The molecular docking study confirmed two binding modes: minor groove binding and threading intercalation with the fluoroquinolone part of the molecule involved in pi stacking interactions and the Ir(III)-containing region positioned within the major or minor groove. Fluorescence spectroscopic data (HSA and apo-Tf titration), together with molecular docking, provided evidence that Ir(III) complexes can bind to the proteins in order to be transferred. All the compounds considered herein were found to bind to the tryptophan residues of HSA within site I (subdomain II A). Furthermore, Ir(III) complexes were found to dock within the apo-Tf binding site, including nearby tyrosine residues.


ACS Omega ◽  
2017 ◽  
Vol 2 (11) ◽  
pp. 8490-8494 ◽  
Author(s):  
Haiyang Gao ◽  
Zhi Zhu ◽  
Xiankai Jiang ◽  
Jun Guo ◽  
Bo Song ◽  
...  

2021 ◽  
Vol 55 (2 (255)) ◽  
pp. 158-164
Author(s):  
Nara H. Petrosyan

The study on the interaction of DNA-specific low-molecular compounds – groove binding material Hoechst 33258 and intercalating ligand methylene blue (MB) with serum albumin has been carried out. The absorption and differential absorption spectra of complexes of the mentioned ligands with protein were obtained. Changes of the absorption and differential absorption spectra indicate the binding of two ligands with albumin. The obtained results indicate that at the interaction with both ligands, the conformational state of the protein alters, though these changes are not similar, since in the case of MB a compactization of the protein folding occurs, while in the case of Hoechst 33258, most apparently, an unfolding of the compact structure takes place as a result of partial loss of helicity of $\alpha$-structures.


Biochemistry ◽  
1996 ◽  
Vol 35 (4) ◽  
pp. 1106-1114 ◽  
Author(s):  
Nadarajah Vigneswaran ◽  
Charles A. Mayfield ◽  
Brad Rodu ◽  
Roger James ◽  
H.-G. Kim ◽  
...  

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