New curcumin-derived ligands and their affinity towards Ga3+, Fe3+ and Cu2+: spectroscopic studies on complex formation and stability in solution

2018 ◽  
Vol 42 (10) ◽  
pp. 7680-7690 ◽  
Author(s):  
Luca Rigamonti ◽  
Giulia Orteca ◽  
Mattia Asti ◽  
Valentina Basile ◽  
Carol Imbriano ◽  
...  
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Physical Properties ◽  
Antiproliferative Activity ◽  
Spectroscopic Studies ◽  
Metal Chelating ◽  
Improved Stability ◽  
Chelating Ability

Chemico-physical properties, metal chelating ability, antiproliferative activity and DNA binding of new curcuminoids with improved stability.

Water soluble palladium(ii) and platinum(ii) acyclic diaminocarbene complexes: solution behavior, DNA binding, and antiproliferative activity

2020 ◽  
Vol 44 (15) ◽  
pp. 5762-5773 ◽  
Author(s):  
Tatiyana V. Serebryanskaya ◽  
Mikhail A. Kinzhalov ◽  
Vladimir Bakulev ◽  
Georgii Alekseev ◽  
Anastasiya Andreeva ◽  
...  
Keyword(s):  
Dna Binding ◽  
Antiproliferative Activity ◽  
Water Soluble ◽  
Solution Behavior ◽  
Antitumor Potential ◽  
Acyclic Diaminocarbene

Water soluble Pd(ii) and Pt(ii)–ADC species synthesized via the metal-mediated coupling of isocyanides and 1,2-diaminobenzene have demonstrated antitumor potential.

scholarly journals Inhibition of Ets-1 DNA Binding and Ternary Complex Formation between Ets-1, NF-κB, and DNA by a Designed DNA-binding Ligand

1999 ◽  
Vol 274 (18) ◽  
pp. 12765-12773 ◽  
Author(s):  
Liliane A. Dickinson ◽  
John W. Trauger ◽  
Eldon E. Baird ◽  
Peter B. Dervan ◽  
Barbara J. Graves ◽  
...  
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Ternary Complex ◽  
Ternary Complex Formation

Antiproliferative Activity of Novel Derivative of Thiopyran on Breast and Colon Cancer Lines and DNA Binding

2012 ◽  
Vol 31 (1) ◽  
pp. 128-134 ◽  
Author(s):  
Mehdi Rajabi ◽  
Mohammad A. Khalilzadeh ◽  
Jamshid Mehrzad
Keyword(s):  
Colon Cancer ◽  
Dna Binding ◽  
Antiproliferative Activity

Functional characterization of the NF-kappa B p65 transcriptional activator and an alternatively spliced derivative

1992 ◽  
Vol 12 (2) ◽  
pp. 444-454
Author(s):  
S M Ruben ◽  
R Narayanan ◽  
J F Klement ◽  
C H Chen ◽  
C A Rosen
Keyword(s):  
Dna Binding ◽  
Complex Formation ◽  
Functional Characterization ◽  
Transcriptional Activator ◽  
Single Amino Acid ◽  
Nf Kappa B ◽  
Mobility Shift ◽  
Activation Domain ◽  
Transcriptional Activator Protein

The NF-kappa B transcription factor complex is composed of two proteins, designated p50 and p65, both having considerable homology to the product of the rel oncogene. We present evidence that the p65 subunit is a potent transcriptional activator in the apparent absence of the p50 subunit, consistent with in vitro results demonstrating that p65 can interact with DNA on its own. To identify the minimal activation domain, chimeric fusion proteins between the DNA binding domain of the yeast transcriptional activator protein GAL4 and regions of the carboxy terminus of p65 were constructed, and their transcriptional activity was assessed by using a GAL4 upstream activation sequence-driven promoter-chloramphenicol acetyltransferase fusion. This analysis suggests that the boundaries of the activation domain lie between amino acids 415 and 550. Moreover, single amino acid changes within residues 435 to 459 greatly diminished activation. Similar to other activation domains, this region contains a leucine zipper-like motif as well as an overall net negative charge. To identify those residues essential for DNA binding, we made use of a naturally occurring derivative of p65, lacking residues 222 to 231 (hereafter referred to as p65 delta), and produced via an alternative splice site. Gel mobility shift analysis using bacterially expressed p65, p65 delta, and various mutants indicates that residues 222 to 231 are important for binding to kappa B DNA. Coimmunoprecipitation analysis suggests that these residues likely contribute to the multimerization function required for homomeric complex formation or heteromeric complex formation with p50 in that no association of p65 delta with itself or with p50 was evident. However, p65 delta was able to form weak heteromeric complexes with p65 that were greatly reduced in their ability to bind DNA. On the basis of these findings, we suggest that subtle changes within the proposed multimerization domain can elicit different effects with the individual Rel-related proteins and that a potential role of p65 delta may be to negatively regulate NF-kappa B function through formation of nonfunctional heteromeric complexes.

scholarly journals Synthesis, DNA-binding and antiproliferative activity of N-(Nitrogen heterocyclic) norcantharidin acylamide acid

2009 ◽  
Vol 7 (3) ◽  
pp. 569-575 ◽  
Author(s):  
Wen-Zhong Zhu ◽  
Rui-Ding Hu ◽  
Qiu-Yue Lin ◽  
Xiao-Xia Wang ◽  
Xiao-Liang Zheng
Keyword(s):  
Dna Binding ◽  
Cell Line ◽  
Elemental Analysis ◽  
Antiproliferative Activity ◽  
Plasmid Dna ◽  
H Nmr ◽  
Smmc7721 Cell ◽  
Calf Thymus ◽  
Binding Experiment ◽  
Pbr322 Plasmid

AbstractTwo novel norcantharidin acylamide acids (HL1=N-pyrimidine norcantharidin acylamide acid, C12H13N3O4; HL2=N-pyridine norcantharidin acylamide acid, C13H14N2O4) were synthesized by a reaction of norcantharidin(NCTD) with 2-aminopyrimidine and 2-aminopyridine, respectively. Their structures were characterized by elemental analysis, IR, UV and 1 H NMR. Fluorescence titration and viscosity measurements indicated that HL1, HL2 and HL3 (HL3=N-phenyl norcantharidin acylamide acid, C14H15NO4) can bind calf thymus DNA via partial intercalation. The liner Stern-Volmer quenching constant Ksv values for HL1, HL2 and HL3 were 2.05 × 104 L mol−1, 1.15 × 104 L mol−1 and 8.30×103 L mol−1, respectively. Two compounds containing heterocycle of HL1 and HL2 have been found to cleave pBR322 plasmid DNA at physiological pH and temperature. The test of antiproliferation activity showed that the compounds had moderate to strong antiproliferative ability against the tested cell lines except of HL3 against the SMMC7721 cell line. The results indicated that the heterocycle attached to the norcantharidin was favorable to antiproliferative activity. This result was consistent with the DNA binding experiment.

Physical Properties of Human Polynucleotide Kinase:  Hydrodynamic and Spectroscopic Studies†

Biochemistry ◽  
2001 ◽  
Vol 40 (43) ◽  
pp. 12967-12973 ◽  
Author(s):  
Rajam S. Mani ◽  
Feridoun Karimi-Busheri ◽  
Carol E. Cass ◽  
Michael Weinfeld
Keyword(s):  
Physical Properties ◽  
Spectroscopic Studies ◽  
Polynucleotide Kinase
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