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  • 1
    Electronic Resource
    Electronic Resource
    A Simple and Rapid Fluorometric Determination Method of α1-Acid Glycoprotein in Serum Using Quinaldine Red (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 566-570 
    Details
    ISSN: 1573-904X
    Keywords: α1-acid glycoprotein ; fluorescent probe ; quinaldine red ; single radial immunodiffusion method
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract We examined different fluorescent probes suitable for fluorometric determination of α1-acid glycoprotein (AGP) in serum. Quinaldine red (QR) was shown to bind strongly and selectively to AGP. Taking advantage of the enhanced fluorescence of QR in the presence of AGP, we developed a direct method for the determination of serum AGP without removal of other serum proteins such as albumin. AGP concentrations in serum of healthy volunteers and patients correlated well with results from the conventional single radial immunodiffusion (SRID) method (r = 0.93, slope = 1). The newly developed method is faster and has a larger analytical concentration range than the SRID method. This method can also be used to determine AGP in serum of experimental animals, and it can serve to monitor AGP serum concentrations for pharmacokinetic evaluation of basic drugs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018926902083
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  • 2
    Electronic Resource
    Electronic Resource
    Interactions of Aldosterone Antagonist Diuretics with Human Serum Proteins (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 522-526 
    Details
    ISSN: 1573-904X
    Keywords: spironolactone ; canrenone ; drug interaction ; human serum albumin ; α1-acid glycoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. The purpose of this study was to investigate the binding mechanism of aldosterone antagonist diuretics with human serum proteins, human serum albumin (HSA) and α1-acid glycoprotein (AGP), as well as to identify the binding sites of the drugs on these proteins. Methods. Binding activities of spironolactone (SP) and its pharmacologically active metabolite canrenone (CR) to serum and serum protein were examined by ultrafiltration and spectroscopic techniques. The data for the binding of these drugs to HSA were analyzed on the basis of a theoretical model of simultaneous binding of the ligands. Results. The binding percentages of antagonist diuretics SP and CR to human serum proteins were 88.0% and 99.2%, respectively, at therapeutic concentrations. SP bound strongly and almost equally to both HSA and AGP, but CR bound strongly only to HSA. In addition, the displacement results found using fluorescent probes and ultrafiltration methods demonstrated that SP bound to site I, particularly to the warfarin region on HSA, and to the basic binding site on AGP, while CR bound to the warfarin region on HSA. Conclusions. The limited results presented here stress the need for caution on coadministration of acidic drugs which bind to the warfarin region on HSA and basic drugs which bind to AGP with SP and its metabolite CR.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012168020545
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  • 3
    Electronic Resource
    Electronic Resource
    Complex formation of hexakis(2,3,6-tri-O-methyl)-α-cyclodextrin with substituted benzenes in aqueous solution (1988)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 6 (1988), S. 135-142 
    Details
    ISSN: 1573-1111
    Keywords: Permethylated α-cyclodextrin ; induced circular dichroism ; inclusion complex ; host-guest interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The complex formation of hexakis (2,3,6-tri-O-methyl)-α-cyclodextrin with substituted benzenes has been investigated by circular dichroism (CD) spectroscopy. The sign and shape of the CD spectra markedly differ from the spectra of corresponding α-cyclodextrin complexes because of the distorted conformation of the host molecule and/or the difference in the geometry of the host-guest interaction. Enthalpy and entropy changes of the complex formation are determined by using the CD band intensities measured at various temperatures and host concentrations. Negative values of ΔH and ΔS indicate that the hydrophobic interaction is not the major driving force for the complex formation. The guest molecule is suggested to be tightly bound within the host cavity through the induced-fit conformational change of the host molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00663046
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  • 4
    Electronic Resource
    Electronic Resource
    Crystal structures of heptakis(2,3,6-tri-O-methyl)-β-cyclodextrin complexes with (R)- and (S)-Flurbiprofen (1988)
    Springer
    Journal of inclusion phenomena and macrocyclic chemistry 6 (1988), S. 443-460 
    Details
    ISSN: 1573-1111
    Keywords: Methylated cyclodextrin ; inclusion complex ; host-guest interaction ; chiral recognition ; crystal structure ; Flurbiprofen
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Hepatakis(2,3,6-tri-O-methyl)-β-cyclodextrin (TM-β-CDx) forms crystalline complexes with (R)-Flubiprofen (R-FP), C63H112O35C15H13O2F·H2O, and (S)-Flurbiprofen (S-FP), C63H112O35C15H13O2F. The crystal structures were determined by X-ray analysis. Crystals of both compounds are orthorhombic and the space group isP212121 with cell dimensions:a=15.092(2),b=21.714(3), andc=28.269(4) Å for theR-FP complex, anda=15.271(2),b=21.451(3) andc=27.895(3) Å for theS-FP complex. The macrocyclic ring of TM-β-CDx is markedly distorted because of the inability to form intramolecular hydrogen bonds and the steric hindrance involving methyl groups. In both complexes, the phenyl group is inserted into the host cavity from the O(2), O(3) side, which is wider than the O(6) side. The biphenyl moiety ofR-FP is fixed in theR-configuration within the host cavity. The phenyl group ofS-FP is disordered, andR-andS-configurations are statistically distributed with equal probability. TM-β-CDx molecules are stacked along theb axis to form a column structure. The TM-β-CDx molecule is laterally shifted with respect to the column axis, and a half of the guest molecule protrudes outside from the crevis of the column. The carboxyl group ofR-FP forms a hydrogen bond with water located outside the host cavity, while the carboxyl group ofS-FP is hydrogen-bonded to an oxygen atom of an adjacent TM-β-CDx.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00660743
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  • 5
    Electronic Resource
    Electronic Resource
    Drug Binding to α1-Acid Glycoprotein Studied by Circular Dichroism (1989)
    Springer
    Pharmaceutical research 6 (1989), S. 156-159 
    Details
    ISSN: 1573-904X
    Keywords: circular dichroism ; α1-acid glycoprotein ; binding force ; binding site ; protein binding of drugs ; α1-acid glycoprotein binding of acidic and basic drugs
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interactions of acidic and basic drugs with α1-acid glycoprotein (α1-AGP) were investigated using circular dichroism (CD) measurements. Extrinsic Cotton effects were generated by the binding of drugs to α1-AGP. The CD data suggested the presence of a single binding site on the α1-AGP molecule. The induced ellipticities of the acidic drug–α1-AGP system decreased with increasing pH, while the ellipticities for the basic drugs increased with pH. The ellipticities for all drugs were reduced by the addition of fatty acids. Furthermore, the induced ellipticities decreased in the presence of cesium chloride for basic drugs bound to α1-AGP. The extrinsic Cotton effects therefore appear to result from hydrophobic interaction with α1-AGP for the acidic drugs and from hydrophobic and electrostatic interactions for the basic drugs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015936710919
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  • 6
    Electronic Resource
    Electronic Resource
    Reversal of Signs of Induced Cotton Effects of Dicumarol-α1-Acid Glycoprotein Systems by Phenothiazine Neuroleptics Through Ternary Complexation (1992)
    Springer
    Pharmaceutical research 9 (1992), S. 845-849 
    Details
    ISSN: 1573-904X
    Keywords: α1-acid glycoprotein ; induced circular dichroism ; dicumarol ; phenothiazine derivatives ; ternary complex ; binding mode
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interaction of dicumarol and phenothiazine neuroleptics binding to α1-acid glycoprotein (AGP) was investigated by circular dichroism (CD) and equilibrium dialysis. The induced CD spectra of the dicumarol–AGP complex were affected differently by the different substituents of the phenothiazine molecule. The sign of the induced Cotton effect of dicumarol bound to AGP was reversibly changed with the introduction of the propyldimethylamine substituent at position 10 or chloride group at position 2 of the phenothiazine molecule. Chlorpromazine, which contains both of these substituents reversed the sign of the induced Cotton effect with the highest intensity. The addition of trifluoperazine, fluphenazine, and promethazine containing neither of the two substituents generated a new negative CD band. However, the addition of opromazine, which contains sulfoxide at position 5, decreased the CD intensity of the dicumarol–AGP complex without changing the shape of the CD spectra. Equilibrium dialysis studies revealed that the interaction of dicumarol–AGP with phenothiazine derivatives occurred simultaneously, and the interaction followed a cooperative and anticooperative binding model. Further, among the six phenothiazine derivatives that reversed the signs of the induced Cotton effects of the dicumarol–AGP complex, a linear relationship was observed between coupling constants and the difference in the induced optical ellipticity. The opromazine and dicumarol interaction was competitive for a common binding site on the AGP molecule. Removal of sialic acid did not have any effect on this interaction. These data support the hypothesis that the acidic and the basic drug binding sites overlap each other.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015880327911
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