Binding Study of Semotiadil and Levosemotiadil with α1-Acid Glycoprotein Using High-Performance Frontal Analysis

Rosas, Maria Esther Rodriguez; Shibukawa, Akimasa; Yoshikawa, Yuki; Kuroda, Yasuhisa; Nakagawa, Terumichi

doi:10.1006/abio.1999.4266

Cited by 12 publications

(3 citation statements)

References 37 publications

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“…(6) shows that a linear relationship exists between 1/(F•t 0 -V m ) and c f . Therefore, by determining the average breakthrough times t 0 of solute molecules in frontal analysis under different feed solute concentrations c f in feed solutions, their adsorption parameters n t and K SL can be derived from the intercept and slope of Eq.…”

Section: Frontal Analysis Equationmentioning

confidence: 94%

A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

2007

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A simple frontal analysis equation to determine the adsorption parameters of solute molecules on different adsorbents was presented. It gives the relationship between the average breakthrough time and the feed solute concentration, and by using its linear form, two important parameters, the thermodynamic equilibrium constant K SL for solute adsorption on the surface of adsorbent and the number n t of total adsorption sites distributed on the surface of adsorbent, can be simultaneously determined. The frontal analyses for some aromatic hydrocarbons on RP-C 18 reversed-phase medium, and some protein molecules on RP-C 18 reversed-phase, WCX-1 cation-exchange, PEG-400 hydrophobic and Che1ating Sepharose Fast-flow separately chelated with Zn 2＋ or Cu 2＋ media, were separately carried out to test this equation and their adsorption parameters K SL and n t were separately obtained. The results show that all these frontal analysis data can be well described by this frontal analysis equation. For all of these frontal analysis systems, their parameters n t can separately approximately keep constant and they are independent of solute molecules used, while their parameters K SL are dependent upon both of the media packed in frontal analysis column and the solute molecules used.

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Section: Frontal Analysis Equationmentioning

confidence: 94%

A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

2007

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“…Figure 7B was obtained when the total concentration of D-T4 was increased while those of L-T4 and HSA were constant. (15). In (D) , and Ct (D) was calculated from Eq.…”

Section: Enantiomer-enantiomer Interaction Upon T4-hsa Bindingmentioning

confidence: 99%

“…High-performance frontal analysis (HPFA) is a chromatographic method suitable for the analysis of strong drugprotein binding and has several unique features associated with it (13)(14)(15). HPFA is free from the undesirable effects of conventional methods such as for ultrafiltration and dialysis such as adsorption onto or leakage from the membrane.…”

Section: Introductionmentioning

confidence: 99%

High-Performance Frontal Analysis of the Binding of Thyroxine Enantiomers to Human Serum Albumin Binding of Thyroxine Enantiomers to Human Serum Albumin Kimura

et al. 2005

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Both enantiomers were bound to human serum albumin at two high-affinity sites with similar affinities. The binding constant (K) and the number of binding sites on an HSA molecule (n) evaluated from Scatchard plot analysis were K = 1.01 x 10(6)m(-1) and n = 1.90 for L: -thyroxine, and K = 9.71 x 10(5) m(-1) and n = 1.97 for D: -thyroxine. The binding sites were identified using phenylbutazone and diazepam as site-specific probes for sites I and II, respectively, and each enantiomer was found to bind to both sites. Incorporation of a chiral HPLC column into the on-line system permitted the investigation of enantiomer-enantiomer interactions, which revealed that both enantiomers competitively bind to the same binding sites without significant allosteric effects.

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Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

Escuder-Gilabert

Martínez-Gómez

Villanueva-Camañas

et al. 2008

Biomedical Chromatography

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Stereoselectivity in protein binding can have a significant effect on the pharmacokinetic and pharmacodynamic properties of chiral drugs. The investigation of enantioselectivity of drugs in their binding with human plasma proteins and the identification of the molecular mechanisms involved in the stereodiscrimination by the proteins represent a great challenge for clinical pharmacology. In this review, the separation techniques used for enantioselective protein binding experiments are described and compared. An overview of studies on enantiomer-protein interactions, enantiomer-enantiomer interactions as well as chiral drug-drug interactions, including allosteric effects, is presented. The contribution of individual plasma proteins to the overall enantioselective binding and the animal species variability in drug-plasma protein binding stereoselectivity are reviewed.

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Binding Study of Semotiadil and Levosemotiadil with α1-Acid Glycoprotein Using High-Performance Frontal Analysis

Cited by 12 publications

References 37 publications

A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

High-Performance Frontal Analysis of the Binding of Thyroxine Enantiomers to Human Serum Albumin Binding of Thyroxine Enantiomers to Human Serum Albumin Kimura

Microseparation techniques for the study of the enantioselectivity of drug–plasma protein binding

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