Linked Life Data

9090718

Source:http://linkedlifedata.com/resource/pubmed/id/9090718

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-6-17
pubmed:abstractText
We conclude that TRH and its analogues permeate mainly via paracellular routes in this particular clone of Caco-2 cells because variation in lipophilicity, polar surface properties, or hydrogen bonding potential-all influencing the transcellular pathway-do not give meaningful relationships. On the other hand, the variations in molecular size of the TRH analogues were too small to detect any influence on the paracellular transport properties. Further studies concerning the solution conformation and the hydrodynamical radii of the molecules probably give more information about the structure-permeability relationship of TRH transport across Caco-2 cell monolayers. The influence of the structural variations of these 7 TRH analogues on the binding affinity to the di- and tripeptide transporter, using another Caco-2 cell clone, are currently under investigation in our laboratory.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0724-8741
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
246-50
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Effects of peptide structure on transport properties of seven thyrotropin releasing hormone (TRH) analogues in a human intestinal cell line (Caco-2).
pubmed:affiliation
Department of Pharmaceutics and Biopharmacy, Philipps-University of Marburg, Germany.
pubmed:publicationType
Journal Article