Spectroscopic studies on the binding of barbital to bovine serum albumin

Ding, Fei; Pan, Hong; Li, Zhiyuan; Liu, Feng; Sun, Ying

doi:10.1016/j.jlumin.2009.01.011

Cited by 18 publications

(5 citation statements)

References 41 publications

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“…Accordingly, fluorescence characteristics of tyrosine and tryptophan of a protein can be revealed via setting the Dl at 15 and 60 nm, respectively [22][23][24]39]. The effect of STM on the synchronous fluorescence spectrum of BSA is presented in Fig.…”

Section: Conformation Investigationmentioning

confidence: 99%

“…Furthermore, the fluorescent nature of BSA, which is due to the existence of the tryptophan residues, facilitates using fluorescence spectroscopy for investigating the interaction between BSA and nonfluorescent drugs. Also, it has recently been demonstrated that synchronous fluorescence spectroscopy can be conclusively utilized for confirming the formation of protein-drug complex and determining the site of binding [22][23][24].…”

Section: Introductionmentioning

confidence: 99%

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

Bani-Yaseen

2011

Journal of Luminescence

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Section: Conformation Investigationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Bani-Yaseen

2011

Journal of Luminescence

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“…Serum albumin, the most abundant protein constituent in blood plasma [6], plays a fundamental role in the disposition and transportation of various molecules and can react with many different ligands in vivo and in vitro [7]. As the structure of protein determines its important biological functions, the resultant structural alternations due to its interaction with ligands can influence the transport, metabolism and availability of serum albumin for other ligands [8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic Studies on the Interaction of Acid Yellow With Bovine Serum Albumin

Pan

Liu

Qin

et al. 2010

Journal of Luminescence

102

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“…A similar fluorescence quenching profiles were found for both tyrosine and tryptophan residues upon addition of SAB/RA to BSA in the presence and absence of Au NPs, which could be explained that tyrosine and tryptophan residues of BSA might have equal accessibility to SAB/RA. A tyrosine residue such as Tyr-263 is located in domain II of BSA with a hydrophobic environment, and Trp-212 is also located in this domain [ 57 ]. The fluorescence changes suggested that the interaction between drug and BSA may occur in domain II [ 58 ].…”

Section: Resultsmentioning

confidence: 99%

Elucidating the Influence of Gold Nanoparticles on the Binding of Salvianolic Acid B and Rosmarinic Acid to Bovine Serum Albumin

Peng

Qi²,

Su³

et al. 2015

PLoS ONE

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Salvianolic acid B and rosmarinic acid are two main water-soluble active ingredients from Salvia miltiorrhiza with important pharmacological activities and clinical applications. The interactions between salvianolic acid B (or rosmarinic acid) and bovine serum albumin (BSA) in the presence and absence of gold nanoparticles (Au NPs) with three different sizes were investigated by using biophysical methods for the first time. Experimental results proved that two components quenched the fluorescence of BSA mainly through a static mechanism irrespective of the absence or presence of Au NPs. The presence of Au NPs decreased the binding constants of salvianolic acid B with BSA from 27.82% to 10.08%, while Au NPs increased the affinities of rosmarinic acid for BSA from 0.4% to 14.32%. The conformational change of BSA in the presence of Au NPs (caused by a noncompetitive binding between Au NPs and drugs at different albumin sites) induced changeable affinity and binding distance between drugs and BSA compared with no Au NPs. The competitive experiments revealed that the site I (subdomain IIA) of BSA was the primary binding site for salvianolic acid B and rosmarinic acid. Additionally, two compounds may induce conformational and micro-environmental changes of BSA. The results would provide valuable binding information between salvianolic acid B (or rosmarinic acid) and BSA, and also indicated that the Au NPs could alter the interaction mechanism and binding capability of drugs to BSA, which might be beneficial to understanding the pharmacokinetics and biological activities of the two drugs.

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Spectroscopic studies on the binding of barbital to bovine serum albumin

Cited by 18 publications

References 41 publications

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

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

Spectroscopic Studies on the Interaction of Acid Yellow With Bovine Serum Albumin

Elucidating the Influence of Gold Nanoparticles on the Binding of Salvianolic Acid B and Rosmarinic Acid to Bovine Serum Albumin

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