Linked Life Data

12535605

Source:http://linkedlifedata.com/resource/pubmed/id/12535605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-1-21
pubmed:abstractText
The misfolding of the amyloid peptide, which is the result of a well-known alpha-to-beta transition, causes neurodegenerative disorder. Fluorinated alcohols have been described in the literature as potent solvents which can refold the beta-conformation. The present studies demonstrate the effectiveness of differently fluorinated alcohols for the beta-to-alpha refolding process on fibrillar aggregated amyloid beta(1-40). The regenerated helical structure is shown to be maintained in the absence of the fluoroalcohols, a behaviour which was found to contrast with immunoglobulin. We interpret this difference on the basis of the hydrophilic/hydrophobic domains in the amyloid sequence and present some speculations regarding the free-energy levels of the folded states of both proteins. The effect of the -CF(3) group on the observed conformational changes is interpreted as a result of alterations of the hydration shell of the peptides. Moreover, based on the results achieved with fluoroalcohols, we have used novel fluorinated amphiphiles possessing blood-compatibility properties and studied their effect on amyloid beta(1-40). First results point in the direction of a beta-to-alpha transition. Therefore, the use of fluorine groups in the development of new drugs is considered a new possibility requiring further investigation for the prevention of amyloidosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
1645
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6-14
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:12535605-Amino Acid Sequence, pubmed-meshheading:12535605-Amyloid beta-Peptides, pubmed-meshheading:12535605-Amyloidosis, pubmed-meshheading:12535605-Circular Dichroism, pubmed-meshheading:12535605-Drug Design, pubmed-meshheading:12535605-Ethanol, pubmed-meshheading:12535605-Humans, pubmed-meshheading:12535605-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:12535605-Microscopy, Atomic Force, pubmed-meshheading:12535605-Molecular Sequence Data, pubmed-meshheading:12535605-Peptide Fragments, pubmed-meshheading:12535605-Propanols, pubmed-meshheading:12535605-Protein Conformation, pubmed-meshheading:12535605-Protein Folding, pubmed-meshheading:12535605-Protein Structure, Secondary, pubmed-meshheading:12535605-Solutions, pubmed-meshheading:12535605-Trifluoroethanol
pubmed:year
2003
pubmed:articleTitle
Change and stabilization of the amyloid-beta(1-40) secondary structure by fluorocompounds.
pubmed:affiliation
Max-Planck-Institute for Colloids and Interfaces, Campus Golm, D-14476, Potsdam, Germany.
pubmed:publicationType
Journal Article