Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach

Kandagal, P.B.; Ashoka, S.; Seetharamappa, J.; Shaikh, S.M.T.; Jadegoud, Y.; Ijare, Omkar B.

doi:10.1016/j.jpba.2005.11.037

Cited by 505 publications

(200 citation statements)

References 19 publications

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“…The experimental results indicated that quenching of the fluorescence of BSA by febuxostat was probably followed a static as well as dynamic mechanism and the binding reaction was mainly enthalpy driven, where hydrophobic interaction played a major role. The binding nature assumed that the maximum binding occurs in the principal regions of ligand binding domain, located in hydrophobic cavities in the sub domains IIA and IIIA [5,6]. A phenomenon of mixed static and dynamic quenching was observed at both 280 and 293 nm excitation wavelength (λ ex ), whereas emission occurred at λ em =380 nm, which is careful illustrated with modified Stern-Volmer equation.…”

Section: Resultsmentioning

confidence: 97%

“…The extent of binding between drug and protein normally depends on many factors, including nature of drugs, hydrophobicity, electrostatic charge and pH of the drug molecules, etc. Most of the cases, a reversible binding of the drug with different bio-active compound is observed, when they function as carriers [5]. Dose and dosing interval completely depend on binding of drugs with different protein in the body.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 97%

Section: Introductionmentioning

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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“…[2,3] Complex formation between Amantadine and EA is evident from the data UV/Vis absorption spectra.…”

Section: Absorption Characteristics Of Egg Albumin With Amantadinementioning

confidence: 88%

Molecular Modeling and Multispectroscopic Studies of the Interaction of Amantadine With Egg Albumin

Bakkialakshmi¹

2017

WJPPS

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“…Thus, it may be concluded from the CD results that the binding should be associated with a moderate change in the secondary structure of the protein, but does not cause any major alteration, such as protein denaturation. 49,50 Note that α-helix % has an inverse tendency to increase ligand concentration at 222 nm, whereas at 208 nm the results are random (Table 2), because the sample t-DCTN has chiral centers that contribute for the cotton effect in the region at 208 nm.…”

Section: Thermodynamic Parameters and The Main Binding Force Between mentioning

confidence: 99%

A Study of the Interaction Betweentrans-Dehydrocrotonin, a Bioactive Natural 19-nor-Clerodane, and Serum Albumin

Chaves¹,

Soares²,

Maciel³

et al. 2016

Journal of the Brazilian Chemical Society

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Study of the interaction of an anticancer drug with human and bovine serum albumin: Spectroscopic approach

Cited by 505 publications

References 19 publications

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

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

Molecular Modeling and Multispectroscopic Studies of the Interaction of Amantadine With Egg Albumin

A Study of the Interaction Betweentrans-Dehydrocrotonin, a Bioactive Natural 19-nor-Clerodane, and Serum Albumin

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