Linked Life Data

19250644

Source:http://linkedlifedata.com/resource/pubmed/id/19250644

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2009-3-9
pubmed:abstractText
The sequence LPFFD (iAbeta(5)) prevents amyloid-beta peptide (Abeta) fibrillogenesis and neurotoxicity, hallmarks of Alzheimer's disease (AD), as previously demonstrated. In this study iAbeta(5) was covalently linked to poly(ethylene glycol) (PEG) and the activity of conjugates was assessed and compared to the activity of the peptide alone by in vitro studies. The conjugates were characterized by MALDI-TOF. Competition binding assays established that conjugates retained the ability to bind Abeta with similar strength as iAbeta(5). Transmission electron microscopy analysis showed that iAbeta(5) conjugates inhibited amyloid fibril formation, which is in agreement with binding properties observed for the conjugates towards Abeta. The conjugates were also able to prevent amyloid-induced cell death, as evaluated by activation of caspase 3. These results demonstrated that the biological activity of iAbeta(5) is not affected by the pegylation process.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
6
pubmed:volume
380
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
397-401
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Design and biological activity of beta-sheet breaker peptide conjugates.
pubmed:affiliation
LEPAE, Chemical Engineering Department, Faculty of Engineering, University of Porto, Rua Dr. Roberto Frias, 4200-465 Porto, Portugal. sandra.rocha@fe.up.pt
pubmed:publicationType
Journal Article