Spectroscopic studies on the binding of bioactive phenothiazine compounds to human serum albumin

Kandagal, P.B.; Shaikh, S.M.T.; Manjunatha, D. H.; Seetharamappa, J.; Nagaralli, B.S.

doi:10.1016/j.jphotochem.2007.01.021

Cited by 90 publications

(35 citation statements)

References 28 publications

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“…The fluorescence quenching phenomenon of organic molecules using external quenchers in a liquid phase has been widely investigated by various authors to understand the nature of bimolecular reactions taking place both under steady-state and transient conditions [37][38][39][40]. Such studies are of utmost importance in physical, chemical, biological and medical sciences.…”

Section: Quenching Mechanism Of Htf By Tamoxifenmentioning

confidence: 99%

Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods

Sarzehi¹,

Chamani²

2010

International Journal of Biological Macromolecules

163

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Section: Quenching Mechanism Of Htf By Tamoxifenmentioning

confidence: 99%

Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods

Sarzehi¹,

Chamani²

2010

International Journal of Biological Macromolecules

163

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“…Fluorescence quenching is the reduction of quantum yield of fluorescence from a fluorophore induced by a variety of molecular interaction with a quencher molecule [24,25]. An Increase in the concentration of quencher will mask the fluorophore, result in reduction of emitted fluorescence from the fluorophore molecules.…”

Section: Resultsmentioning

confidence: 99%

“…The fluorescence quenching data were analyzed by the well-known Stern-Volmer equation [25]: from equation 1…”

Section: Analysis Of Fluorescence Quenching Of Bsa By Febuxostatmentioning

confidence: 99%

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

Rabbi¹,

Didaruzzaman²,

Sultan³

2015

J Bioanal Biomed

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Citation: Rabbi SNI, Sultan MdZ, Sohel MdD, Sultan MdZ (2015) Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy. J Bioanal Biomed 7: 164-170. doi:10.4172/1948-593X.1000138 Copyright: © 2015 Rabbi SNI, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. AbstractThe interaction of an anti-gout drug, febuxostat was studied with bovine serum albumin (BSA) applying fluorescence quenching method for the first time. Interaction parameter and magnitude of the force indicated for both, dynamic and static quenching in between febuxostat and BSA protein. Thermodynamic studies indicated for both hydrogen and hydrophobic interactions, observed at 280 nm and only hydrophobic at 293 nm excitation wavelength. Negative ΔH o and positive ΔS o , indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant K b at λ ex =280 nm was 3.467 × 10 3 µM -1 and 4.943 × 10 3 µM -1 at 298 and 308 K temperature whereas, 5.54 × 10 3 µM -1 and 4.44 × 10 3 µM -1 was noted during excitation at λ ex =293 nm wavelength. The K b values in different temperatures assumed that the stability of binding increased with the increase of temperature at λ ex =280 nm, but reverse effect was experienced at an excitation wavelength of λ ex =293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K. Study of Interaction between

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“…Dynamic and static quenching can be distinguished by their different dependence on temperature [28]. The results in Table 1 indicate that the probable quenching mechanism of this complex by CT-DNA involves static quenching, because K sv is decreases with increasing temperature [29].…”

Section: Fluorescence Spectroscopymentioning

confidence: 97%

Multispectroscopic DNA interaction studies of a water-soluble nickel(II) complex containing different dinitrogen aromatic ligands

Shahabadi

Kashanian

Khosravi

et al. 2010

Transition Met Chem

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The water-soluble Ni(II) complex, [Ni(bipy) 2 -(phen-dione)](OAc) 2 Á2H 2 O (bipy = 2,2 0 -bipyridine and phendione = 1,10-phenanthroline-5,6-dione) has been synthesized and characterized by physico-chemical and spectroscopic methods. The binding interactions of this complex with calf thymus DNA (CT-DNA) were investigated using fluorimetry, spectrophotometry, circular dichroism and viscosimetry. In fluorimetric studies, the enthalpy and entropy of the reaction between the complex and CT-DNA showed that the reaction is exothermic (DH = -123.9 kJ mol -1 ; DS = -323.5 J mol -1 K -1 ). The competitive binding studies showed that the complex could not release methylene blue completely. The complex showed absorption hyperchromism in its UV-Vis spectrum with DNA. The calculated binding constant, K b obtained from UV-Vis absorption studies was 2 9 10 5 M -1 . Moreover, the complex induced detectable changes in the CD spectrum of CT-DNA, as well as changes in its viscosity. The results suggest that this nickel(II) complex interact with CT-DNA via a groove-binding mode.

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Spectroscopic studies on the binding of bioactive phenothiazine compounds to human serum albumin

Cited by 90 publications

References 28 publications

Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods

Investigation on the interaction between tamoxifen and human holo-transferrin: Determination of the binding mechanism by fluorescence quenching, resonance light scattering and circular dichroism methods

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

Multispectroscopic DNA interaction studies of a water-soluble nickel(II) complex containing different dinitrogen aromatic ligands

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