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  • 1
    Electronic Resource
    Electronic Resource
    Renin Inhibitor: Relationship Between Molecular Structure and Oral Absorption (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 1443-1447 
    Details
    ISSN: 1573-904X
    Keywords: renin inhibitor ; cyclodextrin ; intestinal permeability ; in situ intestinal loop ; oral absorption ; first pass effect
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Common problems in developing renin inhibitors are low solubility, insufficient oral absorption, and fast hepatic clearance. We focused on the molecular structure of renin inhibitors to overcome these problems. Cyclodextrins (CD) improved the low solubility of renin inhibitors, with β-CD showing the best ability to dissolve renin inhibitors. The intestinal absorption of renin inhibitors varied with both their solubility and molecular structure. Coadministration of β-CD improved the intestinal absorption of some renin inhibitors with low solubility as measured by transport into the mesenteric vein in the absorption experiment using the rat intestinal loop. Substitutions at both the N and C terminals was essential for absorption from the small intestine. A naphthyl group at the N-terminal further improved intestinal absorption. A carrier system appeared to be involved in the intestinal absorption of some renin inhibitors. N-methylation at the amide bond of thiazolylalanine suppressed the high hepatic clearance of one of the test compounds 18 which was well absorbed from the small intestine and it improved its oral bioavailability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018948007419
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Renin Inhibitor: Transport Mechanism in Rat Small Intestinal Brush-Border Membrane Vesicles (1994)
    Springer
    Pharmaceutical research 11 (1994), S. 1448-1451 
    Details
    ISSN: 1573-904X
    Keywords: renin inhibitor ; rat intestinal brush-border membrane vesicle ; BBMV ; proton coupled uphill transport ; peptide carrier system
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The transport characteristics of the renin inhibitor ((3S,4S)-4-[N-morpholinoacetyl-(l-naphthyl)-L-alanyl-N-methyl-(4-thiazolyl)-L-alanyl]amino-3-hydroxy-5-cyclohexyl-l-(4-pyridyl)-l-pentanone; CH3-18) in rat small intestinal brush-border membrane vesicles (BBMV) were examined by a rapid filtration technique. The uptake of CH3-18 was markedly stimulated by an inwardly directed H+ gradient (pH 7.5 inside, pH 5.5 outside) and showed an uphill transport. It was competitively inhibited by tripeptides and tetrapeptides, but not by amino acids or dipeptides. A countertransport effect on the uptake of CH3-18 was observed in the vesicle preloaded with a tripeptide. Effects of the fragments of several renin inhibitors were evaluated by their inhibitory and countertransport effects on the uptake of CH3-18. The morpholino group at the N-terminal was found to be important for the uptake of CH3-18.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018900124257
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Epimerization Kinetics of Moxalactam in Frozen Urine and Plasma Samples (1990)
    Springer
    Pharmaceutical research 7 (1990), S. 364-369 
    Details
    ISSN: 1573-904X
    Keywords: moxalactam ; epimerization ; frozen plasma ; frozen urine ; electrolyte ; protein binding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The epimerization of moxalactam (LMOX) in frozen urine and plasma samples was studied during long-term storage. The R/S ratio at equilibrium [(R/S)eq] at −10°C was similar in urine and in rat and human plasma ultrafiltrate but differed from that in water. The (R/S)eq values in human plasma and its ultrafiltrate differed slightly, while they were the same in rat plasma and in its ultrafiltrate. The difference for the human plasma and ultrafiltrate may result from differences in plasma protein binding between R- and S-epimers in the liquid region of the frozen plasma. The change of R/S ratio in frozen human plasma continued below the collapse temperature of LMOX aqueous solution, where the liquid region appeared still to exist as determined by NMR measurement. Consequently, the biological LMOX samples should be preserved at or below −70°C to prevent changes in the R/S ratio.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015815321570
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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