Linked Life Data

8996222

Source:http://linkedlifedata.com/resource/pubmed/id/8996222

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-10
pubmed:abstractText
For the purpose of the brain delivery of peptides, the structural specificity of adsorptive-mediated endocytosis at the blood-brain barrier was studied by measuring transport of a newly synthesized basic peptide 001-C8, H-MeTyr-Arg-MeArg-D-Leu-NH(CH2)aNH2, using primary cultured bovine brain capillary endothelial cells. The apparent uptake of [125I]001-C8 increased time-dependently and reached a steady-state at 60 min. The steady-state uptake of [125I]001-C8 was temperature and concentration dependent and was significantly decreased in the presence of dansylcadaverine, protamine or poly-L-lysine. Uptakes of peptides modified by 1,8-octanediamine, 1,5-pentanediamine, 1,2-ethanediamine or ethylamide and peptides with a free carboxyl terminal were significantly higher than, and similar to, that of [3H]PEG900, respectively. The half-saturation constants and the maximal uptake capacities of these peptides were in the ranges of 0.2 to 134 microM and 1.1 to 408 pmol/mg protein, respectively. These values were correlated with the basicity of the molecules. In conclusion, not the number of constituent amino acids of peptides, but rather the C-terminal structure and the basicity of the molecules are the most important determinants for the uptake by the adsorptive-mediated endocytosis system at the blood brain barrier.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0022-3565
pubmed:author
pubmed:issnType
Print
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
410-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Structure-internalization relationship for adsorptive-mediated endocytosis of basic peptides at the blood-brain barrier.
pubmed:affiliation
Department of Pharmaceutics, Faculty of Pharmaceutical Sciences, Kanazawa University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't