Linked Life Data

16117499

Source:http://linkedlifedata.com/resource/pubmed/id/16117499

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
2005-8-24
pubmed:abstractText
We present the first electrochemical detection, characterization, and kinetic study of the aggregation of Alzheimer's disease (AD) amyloid beta peptides (Abeta-40, Abeta-42) using three different voltammetric techniques at a glassy carbon electrode (GCE). This method is based on detecting changes in the oxidation signal of tyrosine (Tyr) residue. As the peptides aggregate, there are structure conformational changes, which affect the degree of exposure of Tyr to the molecular surface of the peptides. The results show significant differences in the aggregation process between the two peptides, and these correlate highly with established techniques. The method is rapid and label-free, and the principle can be universally applied to other protein aggregation studies related to diseases, such as Huntington's, Parkinson's, and Creutzfeldt Jacob (CJD). This method could also be explored in screening for the effectiveness of AD therapies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0002-7863
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
127
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11892-3
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
A rapid label-free electrochemical detection and kinetic study of Alzheimer's amyloid beta aggregation.
pubmed:affiliation
Department of Biological Science and Biotechnology, School of Material Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Nomi City, Ishikawa 923-1292, Japan. munde@jaist.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't