Interaction of glycyrrhetinic acid, furosemide and hydrochlorothiazide with bovine serum albumin and their displacement interactions: capillary electrophoresis and fluorescence quenching study

Zhou, Neng; Liang, Yi‐Zeng; Wang, Bing; Wang, Ping; Chen, Xian; Zeng, Maomao

doi:10.1002/bmc.923

Cited by 8 publications

(2 citation statements)

References 35 publications

(33 reference statements)

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“…Very few studies have been carried out in which n values derived from the double logarithm plot are compared with those obtained by other techniques. In these studies the former methodology renders unitary slopes irrespective of the number of binding sites estimated by other experimental procedures . These differences are stressed by the data obtained in the present work employing HSA and BSA and the dye Coumarin 343‐TEMPO as solute.…”

Section: Resultsmentioning

confidence: 77%

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Lissi

Calderón

Campos

2013

Photochem & Photobiology

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Changes in the intrinsic protein fluorescence with the additive concentration provide one of the most employed methodologies for the evaluation of the binding constant and the number of binding sites. In the last years, more than 175 studies have been published where the double logarithmic plot shown below is used toward determining the number of equivalent binding sites (n). Log [(F° - F)/F] = log K + n log [Q0 ]. However, the value of n evaluated by this procedure is unrelated to the number of equivalent binding sites; rather it represents the stoichiometry of the binding step. The confusion on the meaning of n arises upon assuming that the binding process is represented by the forward and backward elementary steps shown below, implying that binding of the n solutes takes place simultaneously, i.e. there are no intermediate species. nQ + P ⇆ Qn P. The conclusion that n is unrelated to the number of equivalent binding sites is supported by the fact that in all the systems considered (99% of them) n values are close to one and much smaller than those obtained by ultrafiltration. It is then remarkable, the profusion of publications in peer-reviewed, specialized journals including a conceptual error that confuses Hill's coefficient and/or the stoichiometry of the binding step with the number of independent binding sites. Here, we discuss the origin of this common misconception and provide alternative methods to determine the number of binding sites.

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Section: Resultsmentioning

confidence: 77%

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Lissi

Calderón

Campos

2013

Photochem & Photobiology

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“…To evaluate whether GA can be shielded by the assembly, we studied the assembly’s and disassembly’s absorption with bovine serum albumin (BSA) molecules, which has a strong binding constant with GA molecules . As shown in Figure a, stirring the Au NPs at pH 6.8 with BSA resulted in reduced transparency of the solution significantly after 10 min, and showed a broadening absorption with higher absorbance (Figure S4, Supporting Information), where the agglomerates finally flocculate onto the tube bottom after 5 h. On the contrary, BSA scarcely changed the solution of Au NPs at pH 7.4.…”

Section: Resultsmentioning

confidence: 99%

Shieldable Tumor Targeting Based on pH Responsive Self-Assembly/Disassembly of Gold Nanoparticles

Tian

Yang

Wang

et al. 2014

ACS Appl. Mater. Interfaces

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A new approach to shield/deshield ligands for controllable tumor targeting was reported, which was based on amphiphilic self-assembly and disassembly of gold nanoparticles (Au NPs). Thanks to the excellent pH response of the system, glycyrrhetinic acid (GA) ligands can be buried inside the Au NPs' assembly at normal tissue pH (pH 7.4), while exposed when the nanostructure is disassembled at tumor extracellular pH (pHe 6.8). Hydrophobic GA molecules not only acted as ligands targeting tumor cells but also provided the major interparticle attractive force for Au NPs' assembling. An ordered assembly of Au NPs with regular shape, proper size and ultrasharp pH sensitivity (ΔpH ∼ 0.2) was achieved by fine-tuning of materials modified on Au NPs. Mechanism studies for assembly and disassembly of Au NPs indicated the possibility of a GA shield when the assembly formed, which was further demonstrated by bovine serum albumin absorption and cellular uptake. The assembly/disassembly process was reversible within extrinsic pH changes, which provides a perspective for reversible tumor targeting.

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Study of multiple binding constants of dexamethasone with human serum albumin by capillary electrophoresis–frontal analysis and multivariate regression

et al. 2008

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Studies into the interactions between drugs and human serum albumin (HSA) are extremely important for drug discovery, since HSA behaves as a carrier for external drugs and internal biological molecules. In this paper, to evaluate the pharmacokinetic and pharmacodynamic properties of dexamethasone (DXM), the interaction between DXM and HSA was studied by capillary electrophoresis-frontal analysis (CE-FA). According to the Klotz equation, four binding sites between DXM and HSA were obtained, and the average binding constant was 1.05 x 10(3) M(-1). Furthermore, according to multiple equilibrium theory, based on the assumption that there are two types of binding site, the binding constant at one site was calculated to be 3.539 x 10(3) M(-1), and the average of the other three was 1.234 x 10(3) M(-1). In addition, to obtain the detailed binding information at each binding site, new equations were deduced by multivariate regression. The four binding constants of DXM and HSA were calculated to be 5.558 x 10(1) M(-1), 2.158 x 10(4) M(-1), 7.312 x 10(3) M(-1) and 2.043 x 10(3) M(-1), respectively, which is helpful for detailed studies into the interactions between drugs and proteins with multiple binding sites.

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Interaction of glycyrrhetinic acid, furosemide and hydrochlorothiazide with bovine serum albumin and their displacement interactions: capillary electrophoresis and fluorescence quenching study

Cited by 8 publications

References 35 publications

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Shieldable Tumor Targeting Based on pH Responsive Self-Assembly/Disassembly of Gold Nanoparticles

Study of multiple binding constants of dexamethasone with human serum albumin by capillary electrophoresis–frontal analysis and multivariate regression

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