Fluorescence quenching of BPBD by aniline in benzene–acetonitrile mixtures

Thipperudrappa, J.; Biradar, D.S.; Lagare, M.T.; Hanagodimath, S.M.; Inamdar, Sanjeev R.; Kadadevaramath, J S

doi:10.1016/j.jphotochem.2005.05.016

Cited by 57 publications

(40 citation statements)

References 20 publications

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“…has been studied by several investigators by steady state [1][2][3][4][5][6][7][8] and transient methods [9][10][11][12][13]. In almost all the cases, the experimental results follow the linear Stern-Volmer (S-V) relation and is given by…”

Section: Introductionmentioning

confidence: 99%

“…K SV is the S-V constant and [Q] is the quencher concentration. But in some cases, it has been observed that the experimental results show positive deviation from a linear S-V relation [4][5][6][7][8]. This positive deviation is attributed to various processes like intersystem crossing, formation of charge transfer complexes both at ground and excited states, static and dynamic quenching, etc.…”

Section: Introductionmentioning

confidence: 99%

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Role of solvent polarity on the fluorescence quenching of newly synthesized 7,8-benzo-4-azidomethyl coumarin by aniline in benzene–acetonitrile mixtures

Melavanki

Kusanur

Kulakarni

et al. 2008

Journal of Luminescence

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Role of solvent polarity on the fluorescence quenching of newly synthesized 7,8-benzo-4-azidomethyl coumarin by aniline in benzene–acetonitrile mixtures

Melavanki

Kusanur

Kulakarni

et al. 2008

Journal of Luminescence

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“…To determine the mechanism of binding between BSA and NZ-105, fluorescence intensity data were analyzed by the Stern-Volmer equation (16): ( Equation 2) where F and F 0 are the fluorescence intensity with and without the quencher (drug), K sv the Stern-Volmer quenching constant, and [Q ] the concentration of the drug. If the resulting plots exhibit a good linear relationship, this is generally indicative of the purely collisional quenching process or static quenching process (17).…”

Section: Stern-volmer Analysismentioning

confidence: 99%

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

Wang

Zhao

et al. 2008

Braz J Med Biol Res

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Efonidipine hydrochloride is an antihypertensive and antianginal agent with fewer side effects and is better tolerated in the treatment of hypertension with renal impairment. Its interaction with bovine serum albumin (BSA) is of great use for the understanding of the pharmacokinetic and pharmacodynamic mechanisms of the drug. The binding of efonidipine to BSA was investigated by fluorescence spectroscopy and circular dichroism. BSA fluorescence was quenched by efonidipine, due to the fact that efonidipine quenched the fluorescence of tryptophan residues mainly by the collision mode. The thermodynamic parameters ∆H 0 and ∆S 0 were 68.04 kJ/mol and 319.42 J·mol -1 ·K -1 , respectively, indicating that the hydrophobic interactions played a major role. The results of circular dichroism and synchronous fluorescence measurements showed that the binding of efonidipine to BSA led to a conformational change of BSA. The fraction of occupied sites (θ) for the 8-anilino-1-naphthaleinsulfonic acid (ANS)-BSA system is 85%, whereas for the NZ-105-BSA system, it is 53%, which suggests that the interaction of ANS with BSA is stronger than that of NZ-105 with BSA. Binding studies in the presence of ANS indicated that efonidipine competed with ANS for hydrophobic sites of BSA. The effects of metal ions on the binding constant of the efonidipine-BSA complex were also investigated. The presence of metal ions Zn 2+ , Mg 2+ , Al 3+ , K + , and Ca 2+ increased the binding constant of efonidipine-BSA complex, which may prolong the storage period of NZ-105 in blood plasma and enhance its maximum effects.

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“…Modified Stern-Volmer equation [27] can be applied to resolve such situation, where both static and dynamic quenching are operative, in view of exponential form of the model of the sphere of action, V, equation (2) [30][31][32] or on the basis of quadratic dependence [33][34][35] upon quencher concentration model: from equation 2.…”

Section: Citationmentioning

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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Fluorescence quenching of BPBD by aniline in benzene–acetonitrile mixtures

Cited by 57 publications

References 20 publications

Role of solvent polarity on the fluorescence quenching of newly synthesized 7,8-benzo-4-azidomethyl coumarin by aniline in benzene–acetonitrile mixtures

Role of solvent polarity on the fluorescence quenching of newly synthesized 7,8-benzo-4-azidomethyl coumarin by aniline in benzene–acetonitrile mixtures

Spectroscopic studies on the interaction of efonidipine with bovine serum albumin

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

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