Nucleic Acid Interactions of Unfused Aromatic Cations:  Evaluation of Proposed Minor-Groove, Major-Groove, and Intercalation Binding Modes

1998 ◽  
Vol 120 (40) ◽  
pp. 10310-10321 ◽  
Author(s):  
W. David Wilson ◽  
Farial A. Tanious ◽  
Daoyuan Ding ◽  
Arvind Kumar ◽  
David W. Boykin ◽  
...  
Author(s):  
Stephen D. Jett

The electrophoresis gel mobility shift assay is a popular method for the study of protein-nucleic acid interactions. The binding of proteins to DNA is characterized by a reduction in the electrophoretic mobility of the nucleic acid. Binding affinity, stoichiometry, and kinetics can be obtained from such assays; however, it is often desirable to image the various species in the gel bands using TEM. Present methods for isolation of nucleoproteins from gel bands are inefficient and often destroy the native structure of the complexes. We have developed a technique, called “snapshot blotting,” by which nucleic acids and nucleoprotein complexes in electrophoresis gels can be electrophoretically transferred directly onto carbon-coated grids for TEM imaging.


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.


1977 ◽  
Vol 114 (3) ◽  
pp. 333-365 ◽  
Author(s):  
Henry M. Sobell ◽  
Chun-Che Tsai ◽  
Shri C. Jain ◽  
Steven G. Gilbert

1991 ◽  
Vol 46 (1) ◽  
pp. 37-47 ◽  
Author(s):  
Burt G. Feuerstein ◽  
Loren D. Williams ◽  
Hirak S. Basu ◽  
Laurence J. Marton

Biochemistry ◽  
1980 ◽  
Vol 19 (15) ◽  
pp. 3516-3522 ◽  
Author(s):  
Timothy M. Lohman ◽  
C. Glen Wensley ◽  
Jeffrey Cina ◽  
Richard R. Burgess ◽  
M. Thomas Record

1998 ◽  
Vol 8 (1) ◽  
pp. 9-10 ◽  
Author(s):  
PhilipE Bourne ◽  
Judith Murray-Rust ◽  
JeremyH Lakey

2014 ◽  
Vol 9 (11) ◽  
pp. 933-939 ◽  
Author(s):  
Martin D. Baaske ◽  
Matthew R. Foreman ◽  
Frank Vollmer

Biochemistry ◽  
2012 ◽  
Vol 51 (27) ◽  
pp. 5402-5413 ◽  
Author(s):  
Bruno Macedo ◽  
Thiago A. Millen ◽  
Carolina A. C. A. Braga ◽  
Mariana P. B. Gomes ◽  
Priscila S. Ferreira ◽  
...  

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