Linked Life Data

11513811

Source:http://linkedlifedata.com/resource/pubmed/id/11513811

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2001-8-21
pubmed:abstractText
Proteoliposomes were prepared by making bilayer vesicles from neutral egg yolk lecithin and negatively charged alpha-chymotrypsin that had been previously stearoylated. Interaction of these proteoliposomes with a cationic polymer, poly-(N-ethyl-4-vinylpryidinium bromide) (PEVP) was examined. For comparison purposes, interaction of PEVP with egg lecithin vesicles containing an anionic phospholipid, cardiolipin, was also examined. Binding of PEVP to both types of vesicles was electrostatic in nature with the polymer manifesting a higher affinity to the cardiolipin relative to the enzyme. PEVP had no effect on the permeability of the bilayer membranes to sodium chloride. On the other hand, PEVP increased the transmembrane permeability of the nonionic anti-tumor drug, doxorubicin. The greater the negatively charged component in the membrane, the greater the PEVP effect. Polycation binding to the vesicles was accompanied by clustering of the stearoylated chymotrypsin (sCT) molecules within the membrane. This protein clustering is most likely responsible for the increase in the doxorubicin permeation. Enzymatic activity of the membrane-associated sCT remained unchanged upon PEVP binding. These findings seem relevant to the effects of polyelectrolytes on cellular membranes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
1514
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
139-51
pubmed:dateRevised
2009-1-8
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Interaction of a cationic polymer with negatively charged proteoliposomes.
pubmed:affiliation
Polymer Department, School of Chemistry, Lomonosov Moscow State University, Leninskie Gory, Russia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't