Spectrofluorimetric study on the interaction between antimicrobial drug sulfamethazine and bovine serum albumin

Bani-Yaseen, Abdulilah Dawoud

doi:10.1016/j.jlumin.2011.01.019

Cited by 73 publications

(21 citation statements)

References 36 publications

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“…4 and Table 1 listed the corresponding calculated results with all the correlation coefficient over 0.99. The values of binding constants of ilaprazole to BSA in the presence of metal ions were in the range of 10 4 -10 6 mol L À 1 , which agreed with the common affinities of drugs for serum albumin [2][3][4][5][6]. …”

Section: Tablesupporting

confidence: 59%

“…Therefore, it is important to study the interactions of drug with serum albumin, which determines the pharmacology and pharmacodynamics of drugs, and it is also useful to explain the relationship between the structure and function of drugs. Up to now, many manuscripts have reported the interaction between drugs and serum albumin [2][3][4][5][6]. Moreover, drug-serum albumin interaction always causes interference of the binding of other drugs as the result of overlap of binding sites or conformational changes [7,8].…”

Section: Introductionmentioning

confidence: 99%

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Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Zhang

Shi

Huang

et al. 2011

Journal of Luminescence

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Section: Tablesupporting

confidence: 59%

Section: Introductionmentioning

confidence: 99%

Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Zhang

Shi

Huang

et al. 2011

Journal of Luminescence

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Section: Introductionmentioning

confidence: 99%

“…To date, there have been some reports that describe the interaction of HSA and BSA with sulfonamides assayed by capillary electrophoresis, liquid chromatography, fluorescence technique (18)(19)(20), Fourier transform infra-red spectrometry (FT-IR) (21), and circular dichroism (CD) spectroscopy (22). Zou et al studied the binding of SMX and HSA by utilizing a microdialysis sampling technique combined with liquid chromatography (18); Abdulilah Dawoud Bani-Yaseen studied the interaction between sulfamethazine and BSA using fluorescence techniques.…”

Section: Introductionmentioning

confidence: 99%

“…The fluorescence emission data were analyzed by applying Stern-Volmer analysis. Binding constants, number of binding sites and the thermodynamic parameters were determined by applying the Scatchard method and Van 't Hoff plot (20). Nandibewoor et al investigated the binding of SMX and BSA by fluorescence, FT-IR and UV-vis absorption techniques.…”

Section: Introductionmentioning

confidence: 99%

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Molecular modeling and multi‐spectroscopic approaches to study the interaction between antibacterial drug and human immunoglobulin G

et al. 2015

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Mechanistic and conformational studies on the interaction of sulfamethoxazole (SMX) with human immunoglobulin G (HIgG) were performed by molecular modeling and multi-spectroscopic methods. The interaction mechanism was firstly predicted through molecular modeling that confirmed the interaction between SMX and HIgG. The binding parameters and thermodynamic parameters at different temperatures had been calculated according to the Stern-Volmer, Scatchard, Sips and Van 't Hoff equations, respectively. Experimental results showed that the fluorescence intensity of HIgG was quenched by the gradual addition of SMX. The binding constants of SMX with HIgG decreased with the increase of temperature, which meant that the quenching mechanism was a static quenching. Meanwhile, the results also confirmed that there was one independent class of binding site on HIgG for SMX during their interaction. The thermodynamic parameters of the reaction, namely standard enthalpy ΔH(0) and entropy ΔS(0), had been calculated to be -14.69 kJ·mol(-1) and 22.99 J·mol(-1) ·K(-1), respectively, which suggested that the electrostatic and hydrophobic interactions were the predominant intermolecular forces in stabilizing the SMX-HIgG complex. Furthermore, experimental results obtained from three-dimensional fluorescence spectroscopy, UV-vis absorption spectroscopy and circular dichroism (CD) spectroscopy confirmed that the conformational structure of HIgG was altered in the presence of SMX.

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Mechanistic and conformational studies on the interaction of sulfamethazine with human immunoglobulin G by molecular modeling and multi‐spectroscopic approach in vitro

Wang

Cun-fang

et al. 2014

Luminescence

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Binding interaction of sulfamethazine (SMZ) with human immunoglobulin G (HIgG) has been explored under physiological conditions. The interaction mechanism was firstly predicted through molecular modeling which showed that several hydrogen bonds participated in stabilizing the SMZ-HIgG complex. Fluorescence spectroscopy, ultraviolet-visible (UV-vis) light absorption and circular dichroism (CD) spectroscopy were used to analyze the binding site, binding constants and effects of SMZ on HIgG stability and secondary structure. The binding parameters and thermodynamic parameters at different temperatures for the reaction have been calculated according to the Scatchard, Sips and Van 't Hoff equations, respectively. Experimental results showed that the quenching mechanism was a static quenching and there was one independent class of binding site on HIgG for SMZ during their interaction. The thermodynamic parameters of the reaction, namely standard enthalpy ΔH(0) and entropy ΔS(0), had been calculated to be -19.12 kJ · mol(-1) and 20.22 J · mol(-1) · K(-1), respectively, which meant that the electrostatic interaction was the predominant intermolecular force in stabilizing the SMZ - HIgG complex. Moreover, the conformational changes of HIgG in the presence of SMZ were confirmed by three-dimensional fluorescence spectroscopy, UV-vis absorption spectroscopy and CD spectroscopy.

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Spectrofluorimetric study on the interaction between antimicrobial drug sulfamethazine and bovine serum albumin

Cited by 73 publications

References 36 publications

Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Effect of Cu2+ and Fe3+ for drug delivery: Decreased binding affinity of ilaprazole to bovine serum albumin

Molecular modeling and multi‐spectroscopic approaches to study the interaction between antibacterial drug and human immunoglobulin G

Mechanistic and conformational studies on the interaction of sulfamethazine with human immunoglobulin G by molecular modeling and multi‐spectroscopic approach in vitro

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