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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-3-22
pubmed:abstractText
Alzheimer's disease is a degenerative disorder of the brain for which there is no cure or effective treatment. Recent studies suggest that cerebral amyloid plaques are central to the disease process. However, it is not clear which of the species going from the normal soluble amyloid-beta peptide to the mature amyloid plaque is the toxic agent in the brain. Therefore, an attractive therapeutic strategy for Alzheimer's disease is to block the early steps involving the pathological conversion of the soluble peptide into the abnormally folded oligomeric intermediate precursor of the amyloid fibrils. We have engineered synthetic beta-sheet breaker peptides to bind amyloid-beta peptide, stabilize the normal conformation and destabilize the beta-sheet rich structure of the potentially toxic intermediates and hence the formation of amyloid plaques. Results in vitro, in cell culture and in vivo suggest that beta-sheet breaker peptide may be useful for blocking the pathway that lead to the formation of cerebral amyloid deposits. It remains to be proved that inhibition of the defective folding of amyloid-beta peptide and/or amyloid plaque deposition could be beneficial for the therapeutic treatment of Alzheimer's disease.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-1427
pubmed:author
pubmed:issnType
Print
pubmed:volume
176
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
90-5
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Inhibiting the conversion of soluble amyloid-beta peptide into abnormally folded amyloidogenic intermediates: relevance for Alzheimer's disease therapy.
pubmed:affiliation
Serono Pharmaceutical Research Institute, Geneva, Switzerland. Claudio.Soto@serono.com
pubmed:publicationType
Journal Article