Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-10-20
pubmed:abstractText
The amyloid-? peptide (A?) plays a central role in the mechanism of Alzheimer's disease, being the main constituent of the plaque deposits found in AD brains. A? amyloid formation and deposition are due to a conformational switching to a ?-enriched secondary structure. Our strategy to inhibit A? aggregation involves the re-conversion of A? conformation by adsorption to nanoparticles. NPs were synthesized by sulfonation and sulfation of polystyrene, leading to microgels and latexes. Both polymeric nanostructures affect the conformation of A? inducing an unordered state. Oligomerization was delayed and cytotoxicity reduced. The proper balance between hydrophilic moieties and hydrophobic chains seems to be an essential feature of effective NPs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1616-5195
pubmed:author
pubmed:issnType
Electronic
pubmed:day
8
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1152-63
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Randomization of amyloid-?-peptide(1-42) conformation by sulfonated and sulfated nanoparticles reduces aggregation and cytotoxicity.
pubmed:affiliation
Max Planck Institute of Colloids and Interfaces, Wissenschaftspark Golm, Potsdam, Germany. saraiva@mpikg.mpg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't