Molecular recognition between ligands and nucleic acids: DNA binding characteristics of analogs of Hoechst 33258 designed to exhibit altered base and sequence recognition

1991 ◽  
Vol 4 (6) ◽  
pp. 661-669 ◽  
Author(s):  
K. Ekambareswara Rao ◽  
J. William Lown
Keyword(s):  
Dna Binding ◽  
Molecular Recognition ◽  
Nucleic Acids ◽  
Hoechst 33258 ◽  
Binding Characteristics ◽  
Sequence Recognition

Synthesis and sequence-specific DNA binding of a topoisomerase inhibitory analog of Hoechst 33258 designed for altered base and sequence recognition

1992 ◽  
Vol 5 (5) ◽  
pp. 597-607 ◽  
Author(s):  
Malvinder P. Singh ◽  
Tomi Joseph ◽  
Surat Kumar ◽  
Yadagiri Bathini ◽  
J. William Lown
Keyword(s):  
Dna Binding ◽  
Hoechst 33258 ◽  
Sequence Recognition

Molecular recognition between oligopeptides and nucleic acids. Monocationic imidazole lexitropsins that display enhanced GC sequence dependent DNA binding

Biochemistry ◽  
1987 ◽  
Vol 26 (18) ◽  
pp. 5590-5595 ◽  
Author(s):  
Koren Kissinger ◽  
Krzysztof Krowicki ◽  
James C. Dabrowiak ◽  
J. William Lown
Keyword(s):  
Dna Binding ◽  
Molecular Recognition ◽  
Nucleic Acids ◽  
Sequence Dependent

Molecular recognition between oligopeptides and nucleic acids: DNA binding selectivity of a series of 1,2,4-triazole-containing lexitropsins

1991 ◽  
Vol 4 (2) ◽  
pp. 241-252 ◽  
Author(s):  
K. Ekambareswara Rao ◽  
Krzysztof Krowicki ◽  
Guenther Burckhardt ◽  
Christoph Zimmer ◽  
J. William Lown
Keyword(s):  
Dna Binding ◽  
Molecular Recognition ◽  
Nucleic Acids ◽  
Binding Selectivity

scholarly journals Identification of C/EBP basic region residues involved in DNA sequence recognition and half-site spacing preference.

1993 ◽  
Vol 13 (11) ◽  
pp. 6919-6930 ◽  
Author(s):  
P F Johnson
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Dna Sequence ◽  
Leucine Zipper ◽  
Alpha Helix ◽  
Binding Characteristics ◽  
Hybrid Proteins ◽  
Sequence Recognition ◽  
Basic Region ◽  
Half Site

C/EBP and GCN4 are basic region-leucine zipper (bZIP) DNA-binding proteins that recognize the dyad-symmetric sequences ATTGCGCAAT and ATGAGTCAT, respectively. The sequence specificities of these and other bZIP proteins are determined by their alpha-helical basic regions, which are related at the primary sequence level. To identify amino acids that are responsible for the different DNA sequence specificities of C/EBP and GCN4, two kinds of hybrid proteins were constructed: GCN4-C/EBP chimeras fused at various positions in the basic region and substitution mutants in which GCN4 basic region amino acids were replaced by the corresponding residues from C/EBP. On the basis of the DNA-binding characteristics of these hybrid proteins, three residues that contribute significantly to the differences in C/EBP and GCN4 binding specificity were defined. These residues are clustered along one face of the basic region alpha helix. Two of these specificity residues were not identified as DNA-contacting amino acids in a recently reported crystal structure of a GCN4-DNA complex, suggesting that the residues used by C/EBP and GCN4 to make base contacts are not identical. A random binding site selection procedure also was used to define the optimal recognition sequences for three of the GCN4-C/EBP fusion proteins. These experiments identify an element spanning the hinge region between the basic region and leucine zipper domains that dictates optimal half-site spacing (either directly abutted for C/EBP or overlapping by one base pair for GCN4) in high-affinity binding sites for these two proteins.

Identification of C/EBP basic region residues involved in DNA sequence recognition and half-site spacing preference

1993 ◽  
Vol 13 (11) ◽  
pp. 6919-6930
Author(s):  
P F Johnson
Keyword(s):  
Amino Acids ◽  
Dna Binding ◽  
Dna Sequence ◽  
Leucine Zipper ◽  
Alpha Helix ◽  
Binding Characteristics ◽  
Hybrid Proteins ◽  
Sequence Recognition ◽  
Basic Region ◽  
Half Site

C/EBP and GCN4 are basic region-leucine zipper (bZIP) DNA-binding proteins that recognize the dyad-symmetric sequences ATTGCGCAAT and ATGAGTCAT, respectively. The sequence specificities of these and other bZIP proteins are determined by their alpha-helical basic regions, which are related at the primary sequence level. To identify amino acids that are responsible for the different DNA sequence specificities of C/EBP and GCN4, two kinds of hybrid proteins were constructed: GCN4-C/EBP chimeras fused at various positions in the basic region and substitution mutants in which GCN4 basic region amino acids were replaced by the corresponding residues from C/EBP. On the basis of the DNA-binding characteristics of these hybrid proteins, three residues that contribute significantly to the differences in C/EBP and GCN4 binding specificity were defined. These residues are clustered along one face of the basic region alpha helix. Two of these specificity residues were not identified as DNA-contacting amino acids in a recently reported crystal structure of a GCN4-DNA complex, suggesting that the residues used by C/EBP and GCN4 to make base contacts are not identical. A random binding site selection procedure also was used to define the optimal recognition sequences for three of the GCN4-C/EBP fusion proteins. These experiments identify an element spanning the hinge region between the basic region and leucine zipper domains that dictates optimal half-site spacing (either directly abutted for C/EBP or overlapping by one base pair for GCN4) in high-affinity binding sites for these two proteins.

Evaluation of the Anticancer and DNA-Binding Characteristics of Dichloro(diimine)zinc(II) Complexes

Chemistry ◽  
2021 ◽  
Vol 3 (4) ◽  
pp. 1178-1188
Author(s):  
Bandar A. Babgi ◽  
Doaa Domyati ◽  
Magda H. Abdellattif ◽  
Mostafa A. Hussien
Keyword(s):  
Dna Binding ◽  
Binding Constants ◽  
Docking Study ◽  
Binding Mode ◽  
Molecular Docking Study ◽  
Binding Characteristics ◽  
Anticancer Properties ◽  
Amino Phenol ◽  
Donor Acceptor ◽  
Diimine Complexes

Several metal diimine complexes have been reported to possess anticancer properties. To evaluate the anticancer properties of tetrahedral zinc(II) diimine complexes, six complexes were synthesized with the general formula M(N^N)Cl2 {where M = Zn, Pt and N^N = 2,2’-biquinoline (1), 2,2’-dipyridylketone (2) and 4-((pyridine-2-ylmethylene)amino)phenol (3)}. In general, the intrinsic DNA-binding constants for the different compounds exhibited values within close proximity; the changes in the viscosity of the CT-DNA upon binding to the compounds suggest intercalation-binding mode. Molecular docking study predicted that complexes containing the highly planar ligand 2,2’-biquinoline are capable to establish π–π interactions with nucleobases of the DNA; the other four complexes engaged in donor–acceptor interactions with DNA nucleobases. The six complexes and two reference drugs (cisplatin and sunitinib) were tested against two cancer cell lines (COLO 205 and RCC-PR) and one normal cell line (LLC-MK2), highlighting the better performance of the zinc(II) complexes compared to their platinum(II) analogues. Moreover, zinc(II) complexes have higher selectivity index values than the reference drugs, with promising anticancer properties.

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