Study of the interactions between fluoroquinolones and human serum albumin by affinity capillary electrophoresis and fluorescence method

Zhang, Liwei; Wang, Kun; Zhang, Xin‐Xiang

doi:10.1016/j.aca.2007.09.021

Cited by 91 publications

(59 citation statements)

References 45 publications

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“…Several CE approaches have been developed for the study of drug-protein interactions, such as ACE [14], vacancy peak [19], Hummel-Dreyer method [20], vacancy ACE [21] and FA [22]. FA seems to be one of the most favorable for drug-binding studies due to its greater simplicity, speed and versatility to study multiple equilibrium [19].…”

Section: Introductionmentioning

confidence: 99%

“…Several methods have been applied to drug-proteinbinding studies, including equilibrium dialysis [5][6][7], ultrafiltration [6,7], ultracentrifugation [6], gel filtration [6], microdialysis [8], circular dichroism [9], fluorescence spectrometry [10], HPLC, especially high-performance frontal analysis (FA) [11] and high-performance affinity chromatography [12,13], and CE-based methods [9,14]. CE is the most recently developed technique for drug-protein-binding studies.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of interaction between doxycycline and human serum albumin by capillary electrophoresis‐frontal analysis

Sun

2009

Electrophoresis

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The binding of doxycycline to HSA under simulated physiological conditions (pH 7.4, 67 mM phosphate, I=0.17, drug concentration 100 microM, HSA concentration up to 475 microM, 36.5 degrees C) was studied by CE-frontal analysis. The number of primary binding sites, binding constant and physiological protein-binding percentage were 1.9, 1.51 x 10(3) M(-1) and 59.80%, respectively. In addition, the thermodynamic parameters including enthalpy change (DeltaH), entropy change (DeltaS) and free energy change (DeltaG) of the reaction were obtained in order to characterize the acting forces between doxycycline and HSA. Furthermore, to better understand the nature of doxycycline-HSA binding and to get information about potential interaction with other drugs, displacement experiments were performed. The results showed that doxycycline binds at site II of HSA.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of interaction between doxycycline and human serum albumin by capillary electrophoresis‐frontal analysis

Sun

2009

Electrophoresis

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“…The values of n approximately equal to 1 manifest the existence of only one binding site of AEPI with ctDNA. Small molecules form complexes with biomacromolecules, such as DNA and protein, mainly through four forces: electrostatic force, van der Waals force, hydrophobic interaction, hydrogen bonding, etc [22]. The thermodynamic parameters, free energy change (ΔG), enthalpy change (ΔH), and entropy change (ΔS) of the binding reaction can provide evidence for clarifying interaction modes.…”

Section: Binding Constants and Binding Forcesmentioning

confidence: 99%

Interaction of Anthracycline 3′-azido-epirubicin with Calf Thymus DNA via Spectral and Molecular Modeling Techniques

Cui

Niu

et al. 2015

J Fluoresc

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Anthracycline antibiotics are extensively applied to clinical antitumor therapy. The binding mode and mechanism of a new anthracycline 3'-azido-epirubicin (AEPI) with calf thymus deoxyribonucleic acid (ctDNA) were investigated employing multiple spectroscopy techniques in Tris-HCl buffer solution (pH 7.4). Effect of pH on the interaction was provided to determine the proper environment for whole research. Iodide quenching studies and fluorescence polarization measurement indicated that ctDNA quenched the fluorescence of AEPI significantly via intercalation binding mode. The binding constants and binding sites for the interaction were calculated. From binding constant dependence on the temperature, static quenching mechanism of AEPI by ctDNA was confirmed based on the Stern-Volmer equation. Additionally, the thermodynamic parameters for the reaction revealed that the van der Waals force and hydrogen bonding were the main acting forces in the binding process. Molecular modeling result indicated that the hydrogen bonding played a major role in the binding of AEPI to ctDNA.

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“…The thermodynamic parameters for the complexation of Pr 3+ : Amino acid and Ca 2+ ion is evaluated using Van't Hoff plot [12] It can be seen that there is an increase of absorbance and intensity with time. Both hypersensitive and pseudohypersensitive transitions of Pr(III) display significant changes during complexation, which can be seen from the spectral changes with time.…”

Section: B Methodsmentioning

confidence: 99%

A Probe into the Kinetics of the Interaction of Pr(III) Ions with Some Selected Amino Acids: A 4f-4f Transition Spectral Study

Moaienla¹,

Bendangsenla²,

Devi³

2014

AMSA

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Study of the interactions between fluoroquinolones and human serum albumin by affinity capillary electrophoresis and fluorescence method

Cited by 91 publications

References 45 publications

Characterization of interaction between doxycycline and human serum albumin by capillary electrophoresis‐frontal analysis

Characterization of interaction between doxycycline and human serum albumin by capillary electrophoresis‐frontal analysis

Interaction of Anthracycline 3′-azido-epirubicin with Calf Thymus DNA via Spectral and Molecular Modeling Techniques

A Probe into the Kinetics of the Interaction of Pr(III) Ions with Some Selected Amino Acids: A 4f-4f Transition Spectral Study

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