Design and binding of a distamycin A analog to d(CGCAAGTTGGC).cntdot.d(GCCAACTTGCG): synthesis, NMR studies, and implications for the design of sequence-specific minor groove binding oligopeptides

1992 ◽  
Vol 114 (15) ◽  
pp. 5911-5919 ◽  
Author(s):  
Tammy J. Dwyer ◽  
Bernhard H. Geierstanger ◽  
Yadagiri Bathini ◽  
J. William Lown ◽  
David E. Wemmer
Keyword(s):  
Minor Groove ◽  
Minor Groove Binding ◽  
Groove Binding ◽  
Nmr Studies ◽  
Distamycin A

Two-dimensional NMR studies of d(GGTTAATGCGGT).cntdot.d(ACCGCATTAACC) complexed with the minor groove binding drug SN-6999

Biochemistry ◽  
1992 ◽  
Vol 31 (18) ◽  
pp. 4406-4413 ◽  
Author(s):  
Shiow Meei Chen ◽  
Werner Leupin ◽  
Mark Rance ◽  
Walter J. Chazin
Keyword(s):  
Minor Groove ◽  
Minor Groove Binding ◽  
Two Dimensional ◽  
Groove Binding ◽  
Nmr Studies

NMR studies of the complex between the decadeoxynucleotide d(GCATTAATGC)2 and a minor-groove-binding drug

Biochemistry ◽  
1986 ◽  
Vol 25 (20) ◽  
pp. 5902-5910 ◽  
Author(s):  
Werner Leupin ◽  
Walter J. Chazin ◽  
Sven Hyberts ◽  
William A. Denny ◽  
Kurt Wuethrich
Keyword(s):  
Minor Groove ◽  
Minor Groove Binding ◽  
Groove Binding ◽  
Nmr Studies ◽  
A Minor

scholarly journals The minor-groove binding DNA-ligands netropsin, distamycin A and berenil cause polyploidisation via impairment of the G2 phase of the cell cycle.

1990 ◽  
Vol 15 (3) ◽  
pp. 151-157 ◽  
Author(s):  
Martin Poot ◽  
Katrin Kausch ◽  
Julia Köhler ◽  
Thomas Haaf ◽  
Holger Hoehn
Keyword(s):  
Cell Cycle ◽  
Minor Groove ◽  
Minor Groove Binding ◽  
Groove Binding ◽  
Distamycin A ◽  
G2 Phase

Interactions Between a Symmetrical Minor Groove Binding Compound and DNA Oligonucleotides: 1H and 19F NMR Studies

1989 ◽  
Vol 7 (1) ◽  
pp. 101-117 ◽  
Author(s):  
Andrew H.-J. Wang ◽  
Sylvain Cottens ◽  
Peter B. Dervan ◽  
James P. Yesinowski ◽  
Gijs A. van der Marel ◽  
...  
Keyword(s):  
Minor Groove ◽  
19F Nmr ◽  
Minor Groove Binding ◽  
Groove Binding ◽  
Nmr Studies ◽  
Dna Oligonucleotides

scholarly journals 1H NMR study of [d(GCGATCGC)]2 and its interaction with minor groove binding 4',6-diamidino-2-phenylindole.

1993 ◽  
Vol 268 (6) ◽  
pp. 3944-3951
Author(s):  
E. Trotta ◽  
E. D'Ambrosio ◽  
N. Del Grosso ◽  
G. Ravagnan ◽  
M. Cirilli ◽  
...  
Keyword(s):  
1H Nmr ◽  
Minor Groove ◽  
Minor Groove Binding ◽  
Groove Binding ◽  
Nmr Study

scholarly journals Interaction between DNA, Albumin and Apo-Transferrin and Iridium(III) Complexes with Phosphines Derived from Fluoroquinolones as a Potent Anticancer Drug

2021 ◽  
Vol 14 (7) ◽  
pp. 685
Author(s):  
Sandra Amanda Kozieł ◽  
Monika Katarzyna Lesiów ◽  
Daria Wojtala ◽  
Edyta Dyguda-Kazimierowicz ◽  
Dariusz Bieńko ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Serum Proteins ◽  
Docking Study ◽  
Minor Groove ◽  
Docking Studies ◽  
Minor Groove Binding ◽  
Binding Modes ◽  
Groove Binding ◽  
Molecular Docking Study ◽  
Threading Intercalation

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.

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