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  • permeability  (3)
  • cell monolayer  (1)
  • 1
    Electronic Resource
    Electronic Resource
    In Vitro/in Vivo Models for Peptide Oral Absorption: Comparison of Caco-2 Cell Permeability with Rat Intestinal Absorption of Renin Inhibitory Peptides (1993)
    Springer
    Pharmaceutical research 10 (1993), S. 1790-1792 
    Details
    ISSN: 1573-904X
    Keywords: peptide ; oral absorption ; in vitro/in vivo correlation ; cell monolayer ; Caco-2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018990602102
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The Influence of Peptide Structure on Transport Across Caco-2 Cells (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 1453-1460 
    Details
    ISSN: 1573-904X
    Keywords: peptide ; transport ; permeability ; lipophilicity ; hydrogen bonding ; cell culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The relationship between structure and permeability of peptides across epithelial cells was studied. Using confluent monolayers of Caco-2 cells as a model of the intestinal epithelium, permeability coefficients were obtained from the steady-state flux of a series of neutral and zwitterionic peptides prepared from D-phenylalanine and glycine. Although these peptides ranged in lipophilicity (log octanol/water partition coefficient) from −2.2 to +2.8, no correlation was found between the observed flux and the apparent lipophilicity. However, a strong correlation was found for the flux of the neutral series and the total number of hydrogen bonds the peptide could potentially make with water. These results suggest that a major impediment to peptide passive absorption is the energy required to break water–peptide hydrogen bonds in order for the solute to enter the cell membrane. This energy appears not to be offset by the favorable introduction of lipophilic side chains in the amino acid residues.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015825912542
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Caco-2 Cell Monolayers as a Model for Drug Transport Across the Intestinal Mucosa (1990)
    Springer
    Pharmaceutical research 7 (1990), S. 902-910 
    Details
    ISSN: 1573-904X
    Keywords: cell culture ; transport ; intestinal mucosa ; permeability ; epithelial
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Human colon adenocarcinoma (Caco-2) cells, when grown on semipermeable filters, spontaneously differentiate in culture to form confluent monolayers which both structurally and functionally resemble the small intestinal epithelium. Because of this property they show promise as a simple, in vitro model for the study of drug absorption and metabolism during absorption in the intestinal mucosa. In the present study, the transport of several model solutes across Caco-2 cell monolayers grown in the Transwell ™ diffusion cell system was examined. Maximum transport rates were found for the actively transported substance glucose and the lipophilic solutes testosterone and salicylic acid. Slower rates were observed for urea, hippurate, and salicylate anions and were correlated with the apparent partition coefficient of the solute. These results are similar to what is found with the same compounds in other, in vivo absorption model systems. It is concluded that the Caco-2 cell system may give useful predictions concerning the oral absorption potential of new drug substances.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015937605100
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    The Influence of Peptide Structure on Transport Across Caco-2 Cells. II. Peptide Bond Modification Which Results in Improved Permeability (1992)
    Springer
    Pharmaceutical research 9 (1992), S. 435-439 
    Details
    ISSN: 1573-904X
    Keywords: peptide ; transport ; permeability ; lipophilicity ; hydrogen bonding ; cell culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract In order to study the influence of hydrogen bonding in the amide backbone of a peptide on permeability across a cell membrane, a series of tetrapeptide analogues was prepared from D-phenylalanine. The amide nitrogens in the parent oligomer were sequentially methylated to give a series containing from one to four methyl groups. The transport of these peptides was examined across confluent monolayers of Caco-2 cells as a model of the intestinal mucosa. The results of these studies showed a substantial increase in transport with each methyl group added. Only slight differences in the octanol–water partition coefficient accompanied this alkylation, suggesting that the increase in permeability is not due to lipophilicity considerations. These observations are, however, consistent with a model in which hydrogen bonding in the backbone is a principal determinant of transport. Methylation is seen to reduce the overall hydrogen bond potential of the peptide and increases flux by this mechanism. These results suggest that alkylation of the amides in the peptide chain is an effective way to improve the passive absorption potential for this class of compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015867608405
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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