Spectroscopic studies on the interaction of pazufloxacin with calf thymus DNA

Xia, Lang; Zhong, Wenying; Huang, Qi; Ni, Kai

doi:10.1016/j.jphotobiol.2008.07.008

Cited by 154 publications

(45 citation statements)

References 14 publications

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“…K q is the quenching rate constant, and Q is the concentration of Tat (49-57). τ 0 is the average lifetime of fluorophore without Tat (49-57), and its value is approximately 10 -8 s [28] .…”

Section: Resultsmentioning

confidence: 99%

Synthesis, DNA-Binding and Antibacterial Activity of the Cell-Penetrating Peptide HIV-1 Tat (49-57)

Lv¹,

Duan²,

Lu³

et al. 2017

pharmaceutical-sciences

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Section: Resultsmentioning

confidence: 99%

Synthesis, DNA-Binding and Antibacterial Activity of the Cell-Penetrating Peptide HIV-1 Tat (49-57)

Lv¹,

Duan²,

Lu³

et al. 2017

pharmaceutical-sciences

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“…To further examine the static interaction, the following equation 3 was employed to calculate the binding constant and number of binding sites [23].…”

Section: Fluorescence Spectrometrymentioning

confidence: 99%

Vitamin D prevents glycation of proteins: an in vitro study

2016

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Human serum albumin (HSA) is an important protein involved in the transport of hormones, fatty acids, drugs, and other macromolecules. Under hyperglycemic conditions, this molecule undergoes irreversible modification that affects its structure and function. In this study, we explored the effect of two forms of vitamin D, a nutraceutical, on glycation modification in HSA. The protein was incubated with a physiologically high concentration of glucose in the presence of vitamin D metabolites. After 21 days, samples were tested for secondary structural changes, side chain modification, and the presence of advanced glycation end products. Vitamin D metabolites could reduce glycation modification, albeit only to a small extent. Interaction studies reveal that Vitamin D interaction with HSA can prevent protein glycation.Keywords: calcitriol; glycation; protein Type 2 Diabetes is a global health issue growing at an unprecedented rate. The disease accounts for 90% of diabetes cases worldwide and is characterized by defects in glucose metabolism [1]. Persistently high blood glucose concentration encountered in diabetes often initiates Maillard reaction which causes nonenzymatic glycation of proteins and yields a plethora of reactive compounds called advanced glycation end products (AGEs) [2].Modification of protein structure and function by AGEs is consistent with the progression of diabetic complications and correlates positively with the severity of conditions like retinopathy, neuropathy, and nephropathy [3]. Once initiated, AGEs formation continues throughout the lifespan of proteins, and cannot be reversed by normalizing hyperglycemia [2,4].Human serum albumin (HSA) frequently undergoes Maillard reaction to from covalently cross-linked composites [3]. In normal adults, 6-10% of lysine chains are modified by nonenzymatic glycation, however, this number increases by 2-3 folds in individuals suffering from diabetes [5]. This may interfere with HSA function [5]. Since HSA is involved in the transportation of several moieties: nutrients, steroids, and a wide variety of drugs this can have detrimental physiological effects [6].Research suggests that vitamin D is involved in controlling AGE-associated damage in both diabetes and heart disorders [7]. Vitamin D is a fat-soluble micronutrient which is produced in the body by UV irradiation of a precursor steroid stored in the skin. The functionally active form of vitamin D, calcitriol, has a wide array of health implications [8]. Multiple studies have demonstrated its ability in limiting oxidative damage and regulating the status of a potent cellular antioxidant-reduced glutathione (GSH) [7]. Vitamin D deficiency is thought to be a risk factor for the development of diabetes; Low vitamin D status is associated with increased insulin resistance, glycated hemoglobin (HbA1c), and AGE formation [9][10][11]. Previous reports have correlated low circulating concentrations of vitamin D with increased risk of diabetic macrovascular and microvascular complications: mainly nephropathy a...

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“…36,37 Electrostatic, hydrogen bonding and hydrophobic interactions generally contribute to the stability of groove binding, 38 whereas intercalative binding 39 is mostly favoured by stacking interaction with the adjacent DNA bases. 40 It is well known that the intercalation binding of linear or flat aromatic molecules into calf thymus (double-stranded) DNA induce large chirality changes and consequently significant effects on their CD spectra.…”

Section: Circular Dichroismmentioning

confidence: 99%

“…49,50 In the presence of DNA, emission quenching of flavonoids may be caused by the fact that, flavonoids being a small hydrophobic molecule and can be absorbed by hydrophobic groups on the surface of DNA.…”

Section: Emission Spectroscopymentioning

confidence: 99%

Interaction of Two Flavonoids With Calf Thymus Dna: A Multi - Spectroscopic, Electrochemical and Molecular Modelling Approach

Prabhakaran

Jeyasundari²,

Vasantha³

et al. 2018

ECB

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Interaction of naturally occurring bioactive flavonoids 5,6,7-trihydroxyflavone (Baicalein) and 7,8-dihydroxyflavone (DHF) binding with calf thymus deoxyribose nucleic acid (dsDNA) was studied by employing UV absorption, fluorescence, circular dichroism, cyclic voltammetric and molecular modeling techniques. All studies were confirmed that the structural changes of DNA binding to the flavonoid. From the CV results positive shift in peak potential and increased peak current of the flavonoid in the presence of DNA and then the fluorescence quenching of DNA-flavonoids system indicated the intercalative mode of binding between flavonoid and DNA. CD studies suggest the conformational changes in DNA upon interaction with the flavonoids. Molecular docking simulation methods are used as tools to delineate the binding mode and probable location of the flavonoids and their effects on the stability and conformation of Ct-(ds) DNA. Furthermore, Baicalein can bind with more potential with Ct-(ds) DNA than DHF. This is helpful to understand the molecular aspects of binding mode and provides direction for the use and the design of new effective therapeutic agents. These results could provide useful information for insight into the pharmacological mechanism of flavonoids.

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Spectroscopic studies on the interaction of pazufloxacin with calf thymus DNA

Cited by 154 publications

References 14 publications

Synthesis, DNA-Binding and Antibacterial Activity of the Cell-Penetrating Peptide HIV-1 Tat (49-57)

Synthesis, DNA-Binding and Antibacterial Activity of the Cell-Penetrating Peptide HIV-1 Tat (49-57)

Vitamin D prevents glycation of proteins: an in vitro study

Interaction of Two Flavonoids With Calf Thymus Dna: A Multi - Spectroscopic, Electrochemical and Molecular Modelling Approach

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