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  • 1
    Electronic Resource
    Electronic Resource
    Conjugation of copper-zinc superoxide dismutase with succinylated gelatin: Pharmacological activity and cell-lubricating function (1993)
    s.l. : American Chemical Society
    Bioconjugate chemistry 4 (1993), S. 490-498 
    Details
    ISSN: 1520-4812
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bc00024a011
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  • 2
    Electronic Resource
    Electronic Resource
    Interaction of Benzothiadiazides with Human Serum Albumin Studied by Dialysis and Spectroscopic Methods (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 1452-1457 
    Details
    ISSN: 1573-904X
    Keywords: benzothiadiazides ; human serum albumin ; electrostatic interaction ; hydrophobic interaction ; binding site
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The interaction of a series of benzothiadiazides with human serum albumin (HSA) was investigated by equilibrium dialysis (ED) and spectroscopic methods including circular dichroism (CD). The primary binding site of benzothiadiazides was designated site II, the diazepam site on the HSA molecule, as indicated by displacement experiments using different site-selective probes. Tyrosine and lysine amino acid residues were probably involved in the binding site of these compounds to HSA. Both electrostatic and hydrophobic interactions were found to play a role in the binding of these compounds to HSA. Among the compounds tested, chlorothiazide had the highest affinity (K1 = 5.5 × 104M−1, K2 = 5.8 × 103 M−1).The primary binding affinity of the compounds for HSA was of the order: chlorothiazide 〉 cyclopenthiazide 〉 polythiazide 〉 ethiazide 〉 trichlormethiazide = methyclothiazde 〉 hydrochlorothiazide. Binding was insensitive to the N-B transition of HSA. The binding site is proposed to consist of a cationic site on the surface of the HSA molecule with a hydrophobic crevice to accommodate the aromatic ring of the compounds. Positions 3 and 7 of the benzothiadiazide molecule is thought to affect the binding affinity to HSA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018952108327
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  • 3
    Electronic Resource
    Electronic Resource
    The Controlled Release of Prednisolone Using Alginate Gel (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 272-277 
    Details
    ISSN: 1573-904X
    Keywords: alginate ; gel beads ; controlled release ; prednisolone ; in vitro/in vivo correlation ; beagle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In a release study of alginate gel beads, swelling and erosion of the beads were observed at pH 6.8, whereas no swelling occurred at pH 1.2. The amount of released prednisolone (PL) was greater at pH 6.8 than at pH 1.2. The lower the ratio of mannuronic acid block to guluronic acid block in alginate, the slower the release of PL. An increase in loaded PL in the beads resulted in a slower release of PL. The decrease in bead size caused a rapid release of PL. The addition of sodium alginate propylene glycol ester elevated the extent of PL release. The plasma profile of PL showed sustained-release behavior after the oral administration of the beads to beagles. Furthermore, the correlation between in vitro release and in vivo absorption of PL for various alginate gel beads was evaluated using deconvolution and convolution methods. The in vivo absorption of PL was correlated with the PL release at pH 1.2, and it differed from that at pH 6.8. The release of PL from alginate gel beads in vivo appeared to occur under conditions that cause little swelling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018963626248
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  • 4
    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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  • 5
    Electronic Resource
    Electronic Resource
    Species Differences of Serum Albumins: I. Drug Binding Sites (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 1607-1612 
    Details
    ISSN: 1573-904X
    Keywords: drug binding site ; human serum albumin ; experimental animal serum albumins ; species difference
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. The purpose of this study was the classification and identification of drug binding sites on albumins from several species in order to understand species differences of both drug binding properties and drug interaction on protein binding. Methods. Binding properties and types of drug-drug interaction on the different albumins were examined using typical site I binding drugs, warfarin (WF) and phenylbutazone (PBZ), and site II binding drugs, ibuprofen (IP) and diazepam (DZ) on human albumin. Equilibrium dialysis was carried out for two drugs and the free concentrations of drugs were then treated using the methods of Kragh-Hansen (Mol. Pharmacol. 34. 160−171, (1988)). Results. Binding affinities of site I drugs to bovine, rabbit and rat albumins were reasonably similar to human albumin. However, interestingly, those to dog albumin were considerably smaller than human albumin. On the other hand, binding parameters of DZ to bovine, rabbit and rat albumins were apparently different from those of human albumin. These differences are best explained by microenvironmental changes in the binding sites resulting from change of size and/or hydrophobicity of the binding pocket, rather than a variation in amino acid residues. Conclusions. We will propose herein that mammalian serum albumins used in this study contain specific drug binding sites: Rabbit and rat albumins contain a drug binding site, corresponding to site I on human albumin, and dog albumin contains a specific drug binding site corresponding to site II on the human albumin molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012138604016
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  • 6
    Electronic Resource
    Electronic Resource
    Mode of Interaction of Loop Diuretics with Human Serum Albumin and Characterization of Binding Site (1996)
    Springer
    Pharmaceutical research 13 (1996), S. 1015-1019 
    Details
    ISSN: 1573-904X
    Keywords: warfarin binding region ; loop diuretics ; human serum albumin ; binding site ; displacement
    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 loop diuretics with HSA and to characterize the binding site on HSA. Methods. Quantitative analysis of potential interaction between ligands bound to HSA was performed by equilibrium dialysis and data for binding of the two ligands to HSA were analyzed on the basis of a theoretical model of simultaneous binding of two ligands. Results. The binding of loop diuretics is dependent upon the N-B transition, conformational change of albumin. Furthermore, from the results of binding of the drugs to modified HSA, the lysine residue seems to be involved in the binding of loop diuretics to HSA. Conclusions. Analysis using models describing independent, competitive, cooperative and anti-cooperative binding led to the conclusion that loop diuretics bind to site I, particularly to the warfarin region on HSA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016098305796
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  • 7
    Electronic Resource
    Electronic Resource
    Covalent Binding Between Bucillamine Derivatives and Human Serum Albumin (1996)
    Springer
    Pharmaceutical research 13 (1996), S. 1317-1321 
    Details
    ISSN: 1573-904X
    Keywords: human serum albumin ; covalent binding ; bucillamine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To clarify the mechanism of covalent binding between human serum albumin (HSA) and drugs containing thiol groups, we studied the interactions between HSA and bucillamine (BA) and its derivatives. Methods. To determine the concentration of HSA-drug conjugate, we used columns of N-methylpyridium polymer cross-linked with ethylene glycol dimethacrylate (4VP-Me), and analyzed the reaction between HSA and B A derivatives kinetically. Following pseudo first-order reaction kinetics, the rate constants of reduction of non-mercaptoalbumin (HNA) to mercaptoalbumin (HMA) (ka) and formation of HSA-drug conjugate (kc) were determined. Results. Formation of HSA-drug conjugate was observed only for drugs containing one thiol group. In compound IV, the plots of ka and kc against pH were found to be linear. The HSA-drug conjugate was affected by various factors such as pKa, pH, temparture and the microenviroment of Cys34. The increases in ka and kc. against pH were mainly due to the increase in mercaptide ion concentration. Further, fatty acid affected the microenviroment of Cys34, which increased HSA-drug formation. Conclusions. Cys34 located in a crevice on the surface of the protein plays an important role on the formation of HSA-drug conjugate. These results may be useful for elucidating the reaction mechanisms between various proteins and thiol compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016057513490
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  • 8
    Electronic Resource
    Electronic Resource
    Covalent Binding of a Bucillamine Derivative with Albumin in Sera from Healthy Subjects and Patients with Various Diseases (1997)
    Springer
    Pharmaceutical research 14 (1997), S. 351-353 
    Details
    ISSN: 1573-904X
    Keywords: covalent binding ; serum albumin ; bucillamine ; mercapto ratio
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. To investigate the difference of pharmacokinetics of thiol-containing drugs in various disease states, we studied the covalent binding of SA3786, a bucillamine derivative, with proteins in patient serum compared with that in healthy serum. Methods. Sera from healthy volunteers and patients of various diseases were supplied by the Japanese Red Cross Kumamoto Hospital. For the formation of conjugate experiments, SA3786 was added to a final concentration of 7 × 10−4M. After 6h incubation at 37°C, HPLC analysis of 5 μ1 aliquots of each sample was performed using a column of N-methylpyridinium polymer (4VP-Me). Results. The extent of HSA-SA3786 conjugate formation was found to be lower in the sera from healthy volunteers (control) than those from patients of various diseases. Especially high reactivity with SA3786 was observed in sera from rheumatic patients and hepatic patients. With the exception of the fraction of mercaptoalbumin (fHMA), none of the parameters showed a good correlation with conjugate formation. Conclusions. The parameter fHMA must be considered to be one of the most important factors in formation of conjugates between plasma protein and thiol compounds. However, other factors may be involved in addition to fHMA although the nature of these factors is not clear.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1012006306915
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  • 9
    Electronic Resource
    Electronic Resource
    Evaluation of Stereoselective Transdermal Transport and Concurrent Cutaneous Hydrolysis of Several Ester Prodrugs of Propranolol: Mechanism of Stereoselective Permeation (1996)
    Springer
    Pharmaceutical research 13 (1996), S. 1524-1529 
    Details
    ISSN: 1573-904X
    Keywords: prodrug ; penetration ; stereoselectivity ; hydrolysis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Purpose. The purpose of this study was to evaluate the stereoselective permeation and concurrent cutaneous hydrolysis of a series of ester prodrugs of propranolol (PL). Methods. In vitro studies were performed across full-thickness, stripped and diisopropylfluorophosphate (DFP) treated skins of hairless mouse with flow-through diffusion cells at 37°C. Results. The permeability coefficients (K p), which were dependent on partition coefficients (PC), of all the prodrugs were markedly increased compared to the parent drug. In full-thickness skin, the (R) caproyl-PL (CR-PL) showed the highest K p, which was about 52-fold greater than that of PL. Most of the more lipophilic prodrugs showed stereoselectivity in K p (R 〉 S). All the prodrugs underwent stereoselective hydrolysis (R 〉 S) during penetration. The prodrugs which showed stereoselectivity in permeation were comparatively lipophilic and showed great differences in hydrolysis percentages between the enantiomers. Permeation studies with stripped skin revealed that prodrugs were more permeable across stratum corneum compared to PL, whereas reverse was happened across viable skin. Although CR-PL showed high stereoselectivity in permeation across full-thickness skin and underwent higher percent of concurrent stereoselective cutaneous hydrolysis, the prodrug showed no stereoselectivity in permeation across DFP, an esterase inhibitor, treated skin and the concurrent cutaneous hydrolysis was also stopped. Conclusions. Lipophilic prodrugs may readily pass the stratum corneum but may not be able to penetrate so easily through the deeper tissues. Unlike the (S) isomers, the (R) isomers of lipophilic prodrugs almost completely converted to propranolol in epidermis and can easily pass through the dermis layer, resulting in stereoselective penetration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1016031629845
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  • 10
    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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