Linked Life Data

9207229

Source:http://linkedlifedata.com/resource/pubmed/id/9207229

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-7-24
pubmed:abstractText
A peptide consisting of 12 amino acids including 3 glutamic acids (LAEL-LAEL-LAEL; 4(3)E) underwent pH-dependent conformational change from random coil to alpha-helix when the pH was decreased from 7.4 to 5.0 in the presence of egg PC. This alpha-helical 4(3)E had higher membrane-perturbation activity at acidic conditions compared with neutral conditions. When 4(3)E was incorporated with plasmid DNA-cationic peptide complex that utilizes an endocytosis pathway for uptake into cultured cells, high transfection efficiency was observed, indicating that 4(3)E can enhance the transfection activity of cationic peptide. It is likely that 4(3)E in the multi-complex of the plasmid DNA and the cationic peptide effectively disrupts the endosomal membrane and increases the population of the complex which could transfer to cytosol. The small lysosome-disruptive peptide is very probably useful as the enhancer molecule for the gene transfer techniques mediated by the endocytosis pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
235
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
726-9
pubmed:dateRevised
2006-5-1
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The enhancing effect of anionic alpha-helical peptide on cationic peptide-mediating transfection systems.
pubmed:affiliation
Department of Applied Chemistry, Faculty of Engineering, Institute of Tropical Medicine, Nagasaki University, Japan.
pubmed:publicationType
Journal Article