Calorimetric and Spectroscopic Studies to Monitor the Interaction of L-Cysteine Functionalized Selenium Nanoparticles with Calf Thymus DNA

2018 ◽  
Vol 24 (8) ◽  
pp. 5624-5628 ◽  
Author(s):  
Riju K Thomas ◽  
S Prasanth ◽  
T. V Vineeshkumar ◽  
C Sudarsanakumar
Keyword(s):  
Binding Sites ◽  
Binding Constant ◽  
Spectrophotometric Titration ◽  
Spectroscopic Studies ◽  
Binding Energies ◽  
Selenium Nanoparticles ◽  
Calf Thymus Dna ◽  
Calf Thymus ◽  
Number Of Binding Sites ◽  
Ct Dna

The focus of the study is to understand the interaction between calf thymus DNA and L-Cysteine capped Selenium nanoparticles (cys-SeNPs) using spectroscopic and calorimetric techniques. The size of the nanoparticles was confirmed using transmission electron microscope (TEM). Isothermal titration calorimerty (ITC) provided the binding energy, the number of binding sites and the thermodynamic parameters. UV-Vis absorption and fluorescence quenching studies established the number of binding sites and binding constant. Stabilization of the ct-DNA in the presence of cys-SeNPs was determined from thermal melting studies. It is confirmed by the spectrophotometric titration and calorimetric studies that, selenium nanoparticles can form a complex with the double–helical DNA. The binding constant of cys-SeNPs with the DNA from fluorescence study was found to be 2.953 × 106 M−1 and is consistent with the value obtained from ITC experiment. The binding energies along with the binding sites symbolize the crucial role of van der Waals forces and hydrogen bonds in the binding of cys-SeNPs with ct-DNA.

scholarly journals DNA Binding and Photocleavage Studies of Cobalt(III) Polypyridine Complexes: [Co(en)2PIP]3+, [Co(en)2IP]3+, and [Co(en)2phen-dione]3+

2007 ◽  
Vol 2007 ◽  
pp. 1-8 ◽  
Author(s):  
Penumaka Nagababu ◽  
S. Satyanarayana
Keyword(s):  
Plasmid Dna ◽  
Emission Spectroscopy ◽  
Spectroscopic Studies ◽  
Calf Thymus Dna ◽  
Dna Melting ◽  
Base Pairs ◽  
Viscosity Measurements ◽  
Calf Thymus ◽  
Polypyridine Complexes ◽  
Ct Dna

In this paper, three complexes of type[Co(en)2PIP]3+(PIP=2-phenylimidazo[4,5-f][1,10,] phenanthroline)(1),[Co(en)2IP]3+(IP=imidazo[4,5-f][1,10,] phenanthroline)(2), and[Co(en)2phen-dione]3+(1,10 phenanthroline 5,6,dione)(3) have been synthesized and characterized by UV/VIS, IR,1HNMR spectral methods. Absorption spectroscopy, emission spectroscopy, viscosity measurements, and DNA melting techniques have been used for investigating the binding of these two complexes with calf thymus DNA, and photocleavage studies were used for investigating these binding of these complexes with plasmid DNA. The spectroscopic studies together with viscosity measurements and DNA melting studies support that complexes 1 and 2 bind to CT DNA(=calf thymus DNA) by intercalation mode via IP or PIP into the base pairs of DNA, and complex 3 is binding as groove mode. Complex 1 binds more avidly to CT DNA than 2 and 3 which is consistent with the extended planar ringπsystem of PIP. Noticeably, the two complexes have been found to be efficient photosensitisers for strand scissions in plasmid DNA.

Surfactant Complex Binding to DNA Interaction Study: Controlling Hydrophobicity in β-Cyclodextrin–DNA Binding Reactions

2020 ◽  
pp. 318-332
Author(s):  
Nagaraj Karuppiah ◽  
◽  
Muthukumaran Pakkirisamy ◽  
Gunasekaran Gladwin ◽  
Keyword(s):  
Dna Interaction ◽  
Spectroscopic Studies ◽  
Calf Thymus Dna ◽  
Aliphatic Chain ◽  
Groove Binding ◽  
Base Pairs ◽  
Surfactant Complex ◽  
Calf Thymus ◽  
Frame Work ◽  
Ct Dna

The interaction of cis-[Co(phen)2(TA)2](ClO4)3, a cationic surfactant complex (phen = 1-10 phenanthroline, TA= Tetradecylamine), with calf thymus DNA has been studied by physici-chemical techniques. The spectroscopic studies together with cyclic voltammetry and viscosity experiments support that the surfactant-cobalt(III) complex binds to calf thymus DNA (CT DNA) by intercalation through the aliphatic chain present in the complex into the base pairs of DNA. The presence of phenanthroline ligand with larger -frame work may also enhance intercalation. Besides the effect of binding of surfactant cobalt(III) complex to DNA in presence of -cyclodextrin has also studied. In presence of -cyclodextrin the binding occur through surface and (or) groove binding. The complex was investigated as one of the potential

scholarly journals Study on the Interaction of 4'-Hydroxychalcones and their Mannich Derivatives with Calf Thymus DNA by TLC and Spectroscopic Methods, a DNA Cleavage Study

2020 ◽  
Vol 14 (1) ◽  
pp. 122-131
Author(s):  
Zsuzsanna Rozmer ◽  
Aline Bernardes ◽  
Caridad N. Pérez ◽  
Pál Perjési
Keyword(s):  
Cell Lines ◽  
Dna Cleavage ◽  
Binding Constant ◽  
Spectroscopic Method ◽  
Spectrophotometric Titration ◽  
Mannich Bases ◽  
Calf Thymus Dna ◽  
Cleavage Activity ◽  
Dna Cleavage Activity ◽  
Calf Thymus

Background: Phenolic Mannich bases derived from hydroxychalcones show remarkable cytotoxic potencies towards cancer cell lines. However, the exact mechanism of action is still partially uncleared. Objective: Interaction of two hydroxychalcones and their Mannich derivatives with calf thymus DNA (ctDNA) has been investigated. Methods: Thin-layer chromatography and UV-Vis spectroscopic method were used for studying the interaction. The binding constant has been determined by UV-Vis spectrophotometric titration. The DNA cleavage activity of the compounds was studied by agarose gel electrophoresis. Results: Interaction of the compounds with ctDNA exhibited relatively high intrinsic binding constant (4-5x104 M-1). The results indicate existence of weak, non-covalent interactions between the investigated derivatives with ctDNA. Some compounds showed a slight DNA cleavage activity with pBR322. Conclusion: The obtained results provide additional knowledge on the previously documented cytotoxicity against tumor cell lines of the hydroxychalcones and their Mannich-derivatives.

Spectroscopic studies on the interaction of alpha‐eleostearic acid with calf thymus DNA

2019 ◽  
Vol 66 (10) ◽  
pp. 1381-1388
Author(s):  
Yufeng Liu ◽  
Baixin Zhang ◽  
Xiaomei Chen ◽  
Zhian Guo ◽  
Yi Wang ◽  
...  
Keyword(s):  
Eleostearic Acid ◽  
Spectroscopic Studies ◽  
Calf Thymus Dna ◽  
Calf Thymus

Cu(ii)-induced twisting of the biphenyl core: exploring the effect of structure and coordination environment of biphenyl-based chiral copper(ii) complexes on interaction with calf-thymus DNA

2020 ◽  
Vol 44 (46) ◽  
pp. 20275-20284
Author(s):  
Soumen Ghosh ◽  
Mehebub Ali Khan ◽  
Arghyadeep Bhattacharyya ◽  
Md. Akhtarul Alam ◽  
Ennio Zangrando ◽  
...  
Keyword(s):  
Optically Active ◽  
Calf Thymus Dna ◽  
Coordination Environment ◽  
Calf Thymus ◽  
Ct Dna ◽  
Effect Of Structure

Biphenyl core-based clip-like receptors get twisted after complexation with Cu2+. The extent of interaction of the optically active complexes with ct-DNA varies depending on the structure and coordination environment.

Interaction of a synthesized pyrene based fluorescent probe with CT-DNA: spectroscopic, thermodynamic and molecular modeling studies

RSC Advances ◽  
2016 ◽  
Vol 6 (96) ◽  
pp. 93335-93342 ◽  
Author(s):  
Soumen Ghosh ◽  
Abdulla Al Masum ◽  
Aniruddha Ganguly ◽  
Md. Akhtarul Alam ◽  
Md. Maidul Islam ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Fluorescent Probe ◽  
Water Soluble ◽  
Calf Thymus Dna ◽  
Modeling Studies ◽  
Calf Thymus ◽  
Molecular Modeling Studies ◽  
Ct Dna

The present study demonstrates the synthesis of a new pyrene based water soluble fluorescent probe and its interaction with Calf-thymus DNA.

The Binding Of 125I-Von Willebrand Factor To Human Platelets In The Presence Of Ristocetin

1981 ◽  
Author(s):  
P Silber ◽  
T H Finlay
Keyword(s):  
Von Willebrand Factor ◽  
Binding Sites ◽  
Binding Constant ◽  
Specific Binding ◽  
Human Platelets ◽  
Scatchard Analysis ◽  
Binding Data ◽  
Number Of Binding Sites ◽  
Von Willebrand ◽  
Willebrand Factor

The effect of ristocetin on the binding of 125I-porcine von Willebrand factor to human platelets was studied. Previously, we had shown that 125I-porcine von Willebrand factor binds to human platelets in the absence of ristocetin. The present work demonstrates that binding is stimulated by ristocetin and this stimulation is maximal at a ristocetin concentration of 2 mg/ml. At a ristocetin concentration of 0.5 mg/ml, Scatchard analysis indicates a binding constant of 5.18 × 10-9M and the presence of 105,000 binding sites. This compares with our previous finding, in the absence of ristocetin, of a binding constant of 2.92 × 10-7M and 4760 binding sites. These binding data assume the porcine von Willebrand factor to be a tetramer with a molecular weight of 9 × 105. This study indicates that ristocetin causes tighter binding and increases the number of binding sites on human platelets for porcine von Willebrand factor. Unlabelled porcine von Willebrand factor competitively inhibits the specific binding of the labelled protein and gives a binding constant of 0.17 × 10-9M. Similar results were obtained using human von Willebrand factor.

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