Studies of interacting biochemical systems by flow injection analysis

Miller, James N.; Abdullahi, G.L.; Sturley, H.N.; Gossain, V.; McCluskey, P.L.

doi:10.1016/s0003-2670(00)84455-4

Cited by 13 publications

(5 citation statements)

References 12 publications

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“…The cefaclor, etodolac, sulindac, alpha-tris-(hydroxymethyl)-methylamine (tris) and bovine serum albumin (BSA) were purchased from Sigma-Aldrich Chemie (Steinheim, Germany), the 3b-and 3a-aminotropane derivatives (compounds [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20] were synthesized at the Department of Drug Technology and Pharmaceutical Biotechnology at the Medical University of Warsaw. Ortho-phosphoric acid (H 3 PO 4 ) was purchased from POCH (Gliwice, Poland).…”

Section: Reagentsmentioning

confidence: 99%

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A method for rapid screening of interactions of pharmacologically active compounds with albumin

Majcher

Lewandrowska

Herold

et al. 2015

Analytica Chimica Acta

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Section: Reagentsmentioning

confidence: 99%

“…Also the flow injection analysis was used for studying association constants. In this method the calibration of the system is required prior to measurements [13][14][15][16]. Each of the presented methods has disadvantages and limitations.…”

Section: Introductionmentioning

confidence: 99%

A method for rapid screening of interactions of pharmacologically active compounds with albumin

Majcher

Lewandrowska

Herold

et al. 2015

Analytica Chimica Acta

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“…In fact, the FIG technique has been successfully used for accurate and automated determination of formation constants of various chemical systems − and for the characterization of a variety of chemical systems including acidity constants and proton−ligand equilibria. The FIG technique can also be used to determine binding constants between fluorescent probes and drugs to proteins . It is possible to use the FIG technique to generate concentration profiles for systems such as the inclusion complex formation between β-CD and phenolphthalein, and the incorporation of organic molecules ( p -toluenesulfonic acid and benzophenone) into aqueous micelles.…”

Section: Introductionmentioning

confidence: 99%

Determination of Binding Constants by Flow Injection Gradient Technique

1998

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A new method is based on the flow injection gradient equipped with an acousto-optic tunable filter (AOTF) detector has been developed for the determination of binding constants of substrates with cyclodextrins or micelles. The concentration gradient produced by this method eliminates the need to prepare series of mixtures in which the concentrations of one of the reactants are varied. The fast scanning ability of the AOTF enables the detector to record the whole absorption spectrum of the mixture as it flows through the flow cell. Binding constants can be rapidly determined. The effectiveness of the method was evaluated by determining binding constants of inclusion complex formation between β-cyclodextrin (β-CD) and phenolphthalein and of the incorporation of organic molecules (e.g., p-toluenesulfonic acid (PTS) and benzophenone (BP)) into micelles (CTAB) under steady state condition (no flow) and compared with values determined under the flow injection gradient. The method is particularly effective for charged substrates, e.g., the binding constants obtained between PTS and CTAB and between phenolphthalein and β-CD. Neutral substrate, BP, gives relatively poor accuracy and reproducibility, and these may be due to the adsorption of the substrate onto the flow device.

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“…Over the past few years, the flow injection (FI) technique has been successfully used for the automation of chemical equilibria studies (manipulation of reactants and measurement of the analytical signal). In these applications, concentration gradients were created either by flow rate variation − or through the use of an external mixing chamber. − Using a high-dispersion FI system, a very reproducible and wide concentration gradient of the injected sample into the carrier stream can be achieved. , The use of the FI gradient technique in the spectrophotometric study of the complexation of micromolecules to cyclodextrins has been proposed by our group . In this work, we extend the use of the automated FI gradient technique for the potentiometric study of binding of micromolecules to proteins.…”

mentioning

confidence: 99%

Automated Flow Injection Gradient Technique for Binding Studies of Micromolecules to Proteins Using Potentiometric Sensors: Application to Bovine Serum Albumin with Anilinonaphthalenesulfonate Probe and Drugs

Georgiou

Koupparis

1999

Anal. Chem.

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An automated flow injection (FI) gradient technique is described for the binding study of the potentiometric probe 1-anilino-8-naphthalenesulfonate (ANS) to bovine serum albumin (BSA). Using a single-channel FI system with a mixing chamber and a flow ANS electrode, the binding parameters (binding constant and number of binding sites) were calculated using the Scatchard model. The concentration gradient was calibrated by injecting ANS in the stream, and the binding experiment was performed by injecting ANS-BSA solution in the carrier solution of equal albumin concentration. The equations describing the concentration gradient and the corresponding electrode potential curve are presented. A systematic study of the factors affecting the complexation equilibrium and the electrode response was performed. For the ANS binding to BSA, two binding classes were determined with binding constants of (2.1 +/- 0.3) x 10(5) and (3.3 +/- 0.8) x 10(3) M-1 and 3.8 +/- 0.6 and 10 +/- 2 binding sites per class, respectively, at 27 +/- 1 degrees C, in 0.10 M phosphate pH 7.4. Competitive binding experiments of sulfamethoxazole, salicylate, azapropazone, ketoprofen, and tolmetin to albumin were also performed by monitoring ANS binding inhibition (decrease of apparent binding constant). This technique takes advantage of FI gradients and direct potentiometry and utilizes the total information contained in FI peaks, providing fast and accurate binding information in a wide range of concentration ratios.

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Studies of interacting biochemical systems by flow injection analysis

Cited by 13 publications

References 12 publications

A method for rapid screening of interactions of pharmacologically active compounds with albumin

A method for rapid screening of interactions of pharmacologically active compounds with albumin

Determination of Binding Constants by Flow Injection Gradient Technique

Automated Flow Injection Gradient Technique for Binding Studies of Micromolecules to Proteins Using Potentiometric Sensors: Application to Bovine Serum Albumin with Anilinonaphthalenesulfonate Probe and Drugs

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